Abstract
The chemistry of tryptophan (1) has probably been the object of more intense investigation than that of any other amino acids. This is undoubtedly due to the particular reactivity of the indole nucleus and to the extensive chemistry developed over the years regarding this important and ubiquitous functionality. Only the sulfur amino acids have received comparable attention from chemists and biochemists.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Acheson, R. M.: An Introduction to the Chemistry of Heterocyclic Compounds. Interscience Publ., J. Wiley (1973)
Afghan, B. K., and J. Israeli: Reaction of Metal Nitrilotriacetates with ()-Tryptophan. Bull. Soc. Chim. Fr. 4, 1393–1394 (1969)
Agarwal, K. L., G. W. Kenner, and R. C. Sheppard: Peptides. XXVIII. Synthesis of Ovine-Bovine Gastrin I. J. Chem. Soc. C 6, 954–958 (1969)
Alakhov, YU. B., A. A. Kiryushkin, V. M. Lipkin, and G. W. A. Milne: Butylation of the Tryptophan Indole Ring: a Side-Reaction during the Removal of t-Butyloxycarbonyl and t-Butyl Protecting Group in Peptide Synthesis. J. C. S. Chem. Commun. 406–407 (1970)
Aldrich, J. E., and R. B. Cundall: The Radiation-induced Inactivation of Lysozyme. Int. J. Rad. Biol. 16, 343–358 (1969)
Alexander, N. M.: Oxidation and Oxidative Cleavage of Tryptophanyl Peptide Bonds during Jodination. Biochem. Biophys. Res. Commun. 54, 614–619 (1973)
Alexander, N. M.: Oxidative Cleavage of Tryptophanyl Peptide Bonds during Chemical- and Peroxidase-catalyzed Iodinations. J. Biol. Chem. 249, 1946–1952 (1974)
Allegri, G., and A. DE Antoni: Transamination of Kynurenine. Acta Vitamin. Enzymol. (Milan) 28, 223–242 (1974)
Allen, L. M., and W. R. Grover: Tryptophan Tritiation in Supernatant Malate Dehydrogenase from Pig Heart. Biochem. Biophys. Res. Commun. 41, 1518–1522 (1970)
Andrews, L. J., and L. S. Forster: Protein Difference Spectra. Effect of Solvent and Charge of Tryptophan. Biochemistry 11, 1875–1879 (1972)
Arai, S., M. Abe, M. Yamashita, H. Kato, and M. Fujimaki: Applying Proteolytic Enzymes on Soybean. Viii. Formation of an Indole Derivative by Condensation between Tryptophan and n-Hexanal. Agr. Biol. Chem. 35, 552–559 (1971)
Asquith, R. S., and D. E. Rivett: Studies on the Photooxidation of Tryptophan. Biochim. Biophys. Acta 252,111 116 (1971)
Atassi, M. Z.: Specific Cleavage of Tryptophyl Peptide Bonds with Periodate in Sperm Whale Myoglobin. Arch. Biochem. Biophys. 120, 56–59 (1967)
Atassi, M. Z.: Reaction of Amino Acids and Proteins with Trichloroisocyanuric Acid. Tetrahedron Letters 49, 4893–4896 (1973)
Audern, M., and M. Sheinblatt: Nmr Studies of Cyclic Dipeptides containing Histidine and Tryptophan Residues, in: Peptides, Polypeptides and Proteins (E. R. Blout, F. A. Bovey, M. Goodman, and N. Lotan, Eds.), p. 293–299. New York: J. Wiley (1974)
Auer, H. E.: Far-Ultraviolet Absorption and Circular Dichroism Spectra of LTryptophan and Some Derivatives. J. Amer. Chem. Soc. 95, 3003–3011 (1973)
Aviram, I, and A. Schejter: Modification of the Tryptophanyl Residue of Horse Heart Cytochrome C. Biochim. Biophys. Acta 229, 113–118 (1971)
Avrutskaya, I. A., K. K. Babievskii, M. M. Belikov, E. V. ZaporozHets, and M. YA. FlOshchin: Electrochemical Reduction of Indolylnitroacrylate in Alcohol Solution. Elekrokhimiya 9, 163–1368 (1973)
Baba, Y., A. Arimura, and A. V. Schally: Tryptophan Residue in Porcine LH and Fsh-releasing Hormone. Biochem. Biophys. Res. Commun.45,483–487 (1971)
Bachmayer, H.: Effect of Tryptophan Modification on the Activity of Bacterial and Viral Neuramidase. Febs Lett. 23, 217–219 (1972)
Bajusz, S., K. Medzihradszky, Z. Paley, and ZS. Lang: Total Synthesis of Human Corticotropin (α-Acth). Acta Chim. Acad. Sci. Hung. 52, 335–341 (1967)
Bak, B., C. Dambmann, and F. NicolalSen: Hydrogen-deuterium Exchange in Tryptophan. Acta Chem. Scand. 21, 1674–1675 (1967)
Bak, B., C. Dambmann, F. Nicolaisen, and E. J. Pfdersen: Proton Magnetic Resonance Spectra at 220 MH, of Amino Acids, Porcine and Bovine Insulin and the A and BChains of Bovine Tnsulin I Mol Spect 26 78–97 (1968)
Bak, B., J. Led, and E. J. Pedersen: Isotopic Labeling of Tryptophan and Tryptophan Residues in Polypeptides. Acta Chem. Scand. 23, 3051–3054 (1969)
Barman, T. E., and D. E. Koshland, Jr.: A Colorimetric Procedure for the Quantitative Determination of Tryptophan Residues in Proteins. J. Biol. Chem. 242, 5771–5776 (1967)
Barman, T. E.: Reactivities of the Tryptophan Residues of α-Lactalhumin and Lysozyme to 2-Hydroxy-5-Nitrobenzyl Bromide. J. Mol. Biol. 52, 391–394 (1970)
Barman, T. E., and W. Bagshaw: Modification of the Tryptophan Residues of Bovine α-Lactalbumin with 2-Hydroxy-5-nitrobenzyl Bromide and with Dimethyl (2-hydroxy-5-nitrobenzyl) Sulfonium Bromide. II. Effect on the Specific Protein Activity. Biochim. Biophys. Acta. 278. 491–500 (1972)
Barman, T. E.: Modification of the Tryptophan Residues of Bovine α-Lactalbumin with 2-Hydroxy-5-nitrobenzyl Bromide and with Dimethyl (2-hydroxy-5-nitrobenzyl) Sulfonium Bromide. I. Characterization of the Modified Protein. Biochim. Biophys. Acta 257 (2), 293–313 (1972)
Barth, G., E. Bunnenberg, and C. Djerassi: Magnetic Circular Dichroism Studies. Xix. Determination of the Tyrosine: Tryptophan Ratio in Proteins. Anal. Biochem. 48, 471–479 (1972)
Barth, G., W. Voelter, E. Bunnenberg, and C. Djerassi: Magnetic Circular Dichroism Studies. Xvii. Magnetic Circular Dichroism Spectra of Proteins. A New Method for the Quantitative Determination of Tryptophan. J. Amer. Chem. Soc. 94, 1293–1298 (1972)
Battersby, A. R.: Some Applications of Tritium Labeling for the Exploration of Biochemical Mechanisms. Accounts Chem. Res. 5, 148–154 (1972)
Bayer, E., Bacher, P. Krauss, W. Voelter, G. Barth, E. Bunnenberg, and C. Djerassi: Investigation of Xanthine Oxidase. Magnetic Circular Dichroism Studies. Eur. J. Biochem. 22, 580–584 (1971)
Beacham, J., P. H. Bentley, R. A. Gregory, G. W. Kenner, J. K. Macleod, and R. C. Sheppard: Human Gastrin: Isolation, Structure and Synthesis. Synthesis of Human Gastrin T. Nature 209, 585–586 (1966)
Bello, J.: Thermal Perturbation Difference Spectra of Proteins Containing Tryptophyl Residues. Biochemistry 9, 3562–3568 (1970)
Bello, J., and H. R. Bello: Spectral Studies of Interactions of Detergents with Tryptophyl Compounds. Eur. J. Biochem. 34, 535–538 (1973)
Benassi, C. A.: Aspects of Tryptophan Metabolism in Man. Res. Progress in Organic-Biological and Medicinal Chemistry, Soc. Editoriale Farm. (Milan) 1, 45–81 (1964)
Benassi, C. A., E. Scoffone, and F. M. Veronese: Products Arising in the Performic Oxidation of Tryptophan. Tetrahedron Letters 49, 4389–4393 (1965)
Benassi, C. A., F. M. Veronese, A. DE Antoni, and P. Pajetta: Products Arising from the Performic Acid Oxidation of Tryptophan. Gazz. Chim. Ital. 97, 1–17 (1967)
Bencze, W. L., and K. Schmid: Determination of Tyrosine and Tryptophan in Proteins. Anal. Chem. 25, 1193–1196 (1957)
Ben Ladkar, T., M. H. Brieri, and J. Bolard: Induced Optical Activity in DonorAcceptor Complexes. C. R. Acad. Sci., Sez. B 271, 1201–1203 (1970)
Bergstrand, H.: Isolation and Partial Characterization of Some Proteolytically and Chemically Derived Fragments of Bovine Encephalitogenic Protein. Eur. J. Biochem. 21, 116–124 (1971)
Bewley, T. A., and C. H. LI: Reactivity of the Tryptophan Residues in Lysozyme. Nature 206, 624 (1965)
Bewley, T. A., H. Kawauchi, and C. H. LI: Human Pituitary Growth Hormone. Xxxiii. Comparative Studies of the Single Tryptophan Residue in Human Chorionic Somatotropin and Human Pituitary Growth Hormone. Biochemistry 11, 4179–4187 (1972)
Birkofer, L., and K. Hempel: Synthesis of Tritium-Labeled Amino Acids of High Specific Activity. Chem. Ber. 96, 1373–1381 (1963)
Blake, C. C. F.: A Crystallographic Study of the Oxidation of Lysozyme by Iodine. Proc. Roy. Soc. B 167, 435–438 (1967)
Bloxam, L. D., and W. H. Warren: Error in the Determination of Tryptophan by the Method of Denkla and Dewey. A Revised Procedure. Anal. Biochem. 60, 621–625 (1974)
BoccÙ, E., F. M. Veronese, A. Fontana, and C. A. Benassi: Sulfenyl Halide as Modifying Reagents for Polypeptides and Proteins. Vii. Quantitative Evaluation of Tryptophan and Cysteine Residues in Proteins. Eur. J. Biochem. 13, 188–192 (1970)
BoccÙ, E., F. M. Veronese, A. Fontana, and C. A. Benassi: Studies on the Function of Tryptophan-108 on Lysozyme. Acta Vitam. Enzymologica, (Milan), 28, 75–78 (1975).
Bonnett, R., and R. Holleyhead: Reaction of Tryptophan Derivatives with Nitrite. J. Chem. Soc., Perkin I, 962–964 (1974)
Bovey, F. A., and G. V. D. Tiers: Proton N.M.R. Spectroscopy. V. Studies of Amino Acids and Peptides in Trifluoroacetic Acid. J. Amer. Chem. Soc. 81, 2870–2878 (1959)
Boyd, D. R., J. W. Daly, and D. M. Jerinna: Rearrangement of [1 2H]- and [2-2H]-Naphthalene 1,2-Oxides to 1-Naphthol. Mechanism of the Nih Shift. Biochemistry 11, 1961–1966 (1972) and reference therein.
Boyland, E., P. SiMs, and D. C. Williams: The Oxidation of Tryptophan and Some Related Compounds with Persulphate. Biochem. J. 62, 546–550 (1956)
Bradbury, J. H., and R. S. Norton: Carbon-13 Nmr Spectra of Tryptophan, Tryptophan Peptides and of Native and Denaturated Proteins. Biochim. Biophys. Acta 328, 10–19 (1973)
Bradshaw, R. A., and D. A. Deranleau: Use of N-methylnicotinamide Chloride as a Conformational Probe in Proteins. Identification of the Binding Sites in Chicken Egg-white Lysozyme and a Comparison with Bovine α-Lactalbumin. Biochemistry 9 3310–3315 (1970)
Brand, L., and B. Witholt: Fluorescence Measurements, in: Methods in Enzymology– Enzyme Structure (C. H. W. Hirs, Ed.). 11, 776–856. London-New York: Academi Press 1973
Bredderman, P. J.: Tryptophan Analysis of Proteins in 6 M Guanidine Hydrochloride: Modification for More General Application. Anal. Biochem. 61, 298–301 (1974)
Brieskorn, C. H., and K. Danziger: Color Reaction of Tryptophan and Glyoxilic Acid Sulfuric Acid. Z. Lebensm.-Unters. Forsch. 137, 362–370 (1968)
Broentigam, K. H., and T. Severin: Maillard Reaction. IX. Reaction of Tryptophan with Xylose. Z. Lebensm.-Unters. Forsch. 154, 80–83 (1974)
Broquist, P. H., and J. S. Trupin: Amino Acid Metabolism, Ann. Review Biochem. 35, 231–274 (1966)
Brovetto-Cruz, J., and C. H. LI: Human Pituitary Growth Hormone. Studies of the Tryptophan Residues. Biochemistry 8, 4695–4700 (1969)
Brown, R. D., and B. A. W. Coller: A Theoretical Study of the Chemistry of Furan, Pyrrole, Benzofuran, Indole, Dibenzofuran, and Carbazole. Australian J. Chem. 12. 152–165 (1959)
Brundish, E., D. F. Elliott, and R. Wade: Synthesis of L-Amino Acids and their Derivatives Labelled with Tritium. J. Labelled Compd. 7, 473–493 (1971)
Buckingham, R. H., and A. Pirie: Effect of Light on Lens Proteins in Vitro. Exp. Eye Res. 14, 297–299 (1972)
Buku, A., R. Altmann, and TH. Wieland: Components of the Green Deathcap Amanita phalloides. Xlvi. The Nontoxic Sulfoxide Diastereoisomeric of O-Methylα-amanitin. Liebigs Ann. Chem. 1974, 1580–1586.
Burnett, P. R., and E. H. Eylar: Allergic Encephalomyelitis. Oxidation and Cleavage of the Single Tryptophan Residue of the A1 Protein from Bovine and Human Myelin. J. Biol. Chem. 246, 3425–3430 (1971).
Burstein, Y., and A. Patchornik: Selective Chemical Cleavage of Tryptophanyl Peptide Bonds in Peptides and Proteins. Biochemistry 11, 4641–4650 (1972)
Bye, E., and C. Roemming: Crystal Structure of DL-Tryptophan Formate. Acta Chem. Scand. 27, 471–484 (1973)
Capon, B.: Neighbouring Group Participation. Quarterly Reviews 18, 45–111 (1964)
Casnati, G., A. Dossena, and A. Pochini: Electrophilic Substitution in Indoles: Direct Attack at the 2-Position of 3-Alkylindoles. Tetrahedron Letters 5277–5280 (1972)
Casnati, G., M. Francioni, A. Guareschi, and A. Pochini: Insertion of Isoprene Units into Indole Systems. Tetrahedron Letters 2485–2487 (1969)
Casnati, G., R. Marchelli, and A. Pochini: Rearrangement of 3-alkyl-l-alkylIndoles: A Model Reaction for the Biogenesis of Echinulin-type Compounds. J. Chem. Soc. Perkin I, 754–757 (1974)
Cauzzo, G., and G. Jori: Methylene Blue-photosensitized Conversion of 3-substituted Indoles to β-Carboline Derivatives. J. Org. Chem. 37, 1429–1433 (1972)
Cavanaugh, J. R.: The Rotational Isomerism of the Aromatic Amino Acids by Nuclear Magnetic Resonance. J. Amer. Chem. Soc. 92, 1488–1493 (1970)
Chan, T. L.. and K. A. Schellenberc: Studies on the Presence and Role of Tryptophan in Pig Heart Mitochondrial Malate Dehydrogenase. J. Biol. Chem. 243, 6284–6290 (1968)
Chang, C., and K. Hayashi: Chemical Modification of the Tryptophan Residue in Cobratoxin. Biochem. Biophys. Res. Commun. 37, 841–846 (1969)
Chang, C. C., and C. C. Yang: Immunochemical Studies on Tryptophan Modified Cobratoxin. T’ai-Wan I Hsueh Hui Tsa Chih 71, 381–382 (1972). Chem. Abstr. 78, 14382y (1973)
Chao, L., and E. R. Einstein: Localization of the Active Site Through Chemical Modification of the Encephalitogenic Protein. J. Biol. Chem. 245 (23), 6397–6403 (1970)
Chatterjee, A. K., G. J. Durant, H. Hendrickson. Y. C. Lee, and R. Montgomery: Periodatc Oxidation of Biopolymers. Biochem. Biophys. Res. Commun. 4, 425–430 (1961)
Chibata, I., and S. Yamada: Amino Acids. III. Synthesis of DL-tryptophan. Bull. Agr. Chem. Soc. Japan. 21, 58–67 (1957)
Chibata, I., and S. Yamada: Amino Acids. IV. Enzymic Resolution of DL-tryptophan. Bull. Agr. Chem. Soc. Japan. 21, 62–66 (1967)
Cohen, L.: Group-specific Reagents in Protein Chemistry. Ann. Rev. Biochem. 37, 695–726 (1968)
Cohen, L.: Chemical Modifications as a Probe of Structure and Function, in: The Enzymes (P. D. Boyer, Ed.), Vol. I, 148–212. London-New York: Academic Press. 1970
Cohen, J. S.: Proton Magnetic Resonance Studies of Oligopeptides Containing Aromatic Residues Biochim. Biophys Acta 229, 603–609 (1971)
Coletti-Previero, M. A., A. Previero, and E. Zuckerkandl: Separation of the Proteolytic and Esterasic Activities of Trypsin by Reversible Structural Modifications. J. Mol. Biol. 39, 493–501 (1969)
Cornforth, J. W., R. H. Cornforth, C. E. Dalgliesh, and A. Neuberger: D,L-β-3-oxindolylalanine (DL-Hydroxytryptophan). I. Synthesis. Biochem. J. 48, 591 597 (1951)
Cosani, A., E. Peggion, A. S. Verdini, and M. Terbojevich: Far-Ultraviolet Optical Rotatory Properties of Poly-L-Tryptophan. Part. I. Biopolymers 6, 963–971 (1968)
Collson, A., and T. Yonetani: Oxidation of Cytochrome c Peroxidase with Hydrogen Peroxide. Identification of the Endogenous Donor. Biochem. Biophys. Res. Commun. 49, 391–398 (1972)
CoY, D. H., E. J. CoY, and A. V. Schally: Effect of Simple Amino Acid Replacements on the Biological Function of Luteinising Hormone-Releasing Hormone. J. Med. Chem. 16, 1140–1143 (1973)
Coy, D. H., E. J. Coy, and A. V. Schally: Solid Phase Synthesis of Luteinizing Hormone-Releasing Hormone and its Analogues, in: Methods in Enzymology (B. W. O’Malley and J. G. Hardman, Eds.), 37, part B, 416–423. London-New York: Academic Press 1975
CoY, D. H., E. J. Coy, Y. Hirotsu, J. A. Vilchez-Martinez, A. V. Schally, J. W. Van Nispen, and G. T. Tesser: Investigation of the Role of Tryptophan in the Luteinizing Hormone-Releasing Hormone. Biochemistry 13, 3550–3553 (1974)
Cotrait, M., and Y. Barrans: Structure Cristalline de l’Ester Methyliquc du NAcetyl-L-tryptophane. Acta Cryst. B 30, 510–513 (1974). 92. Cuatrecasas, P., S. Fuchs, and C. B. Anfinsen: Tyrosyl Residues at the Active Site of Staphylococcal Nuclease. Modifications by Tetranitromethane. J. Biol. Chem. 243, 4787–4798 (1968)
Dalgliesh, C. E.: The Synthesis of N-Formyl-DL-Kynurenine and Related Compounds, and Observations on the Synthesis of Kynurenine. J. Chem. Soc. 1952, 137–141.
Dalgliesh, C. E.: Nonspecific Formation of Hydroxylated Metabolites of the Aromatic Amino Acids. Arch. Biochem. Biophys. 58, 214–226 (1955)
Daly, J. W., D. M. Jerina, and B. Witkop: Migration of Deuterim During Hydroxylation of Aromatic Substrates by Liver Microsomes. I. Influence of Ring Substituents. Arch. Biochem. Biophys. 128, 517–527 (1968)
Davey, J. M., A. H. Laird, and J. S. Morley: Polypeptides. Part III. The Synthesis of the C-Terminal Tetrapeptide Sequence of Gastrin, its Optical Isomers, and Acylated Derivatives. J. Chem. Soc. (C), 555–566 (1966)
Denckla, W. D., and H. K. Dewey: The Determination of Tryptophan in Plasma, Liver and Urine. J. Lab. Chim. Med. 69, 160–169 (1967)
Deschreider, A. R., and M. Renard: The Influence of Ultraviolet Rays on the Absorption Spectrum of L-Tryptophan. Bull. Inst. Agron. et Stas. Rech. Gembloux 23, 151–165 (1955), Chem. Abstr. 49, 15482e (1955)
Dickman, S. R., and A. L. Crockett: Reactions of Xanthydrol. IV. Determination of Tryptophan in Blood Plasma and Proteins. J. Biol. Chem. 220, 957–965 (1956)
DiopOH, J., and M. Olomucki: New Protein Reagents. II. 4 Chloro-3,5-dinitrophenacyl Bromide. Biochim. Biophys. Acta 263, 220–225 (1972)
Donovan, J. W.: Ultraviolet Difference Spectroscopy. New Techniques and Applications, in: Methods in Enzymology (C. H. W. Hirs and S. N. Timasheff, Eds.). 27, 497–525. London-New York: Academic Press. 1973
Dopheide, T. A. A., and W. M. Jones: Studies on the Tryptophan Residues in Porcine Pepsin. J. Biol. Chcm. 243, 3906–3911 (1968)
Eckstein, H., G. Barth, R. E. Linder, E. Bunnenberg, and C. Djerassi: Untersuchungen des Magnetischen Zirkulardichroisin. Xxiv. Kinetische Untersuchungen der Tryptophanoxidation in Proteinen. Liebigs Ann. Chern. 1974, 990–995.
Edelhoch, H.: Spectroscopic Determination of Tryptophan and Tyrosine in Proteins- Biochemistry 6, 1948–1954 (1967)
Edelhoch, H., R. E. Lippoldt, and M. Wilchek: The Circular Dichroism of Tyrosyl and Tryptophanyl Diketopiperazines. J. Biol. Chem. 243, 4799–4805 (1968)
Edwards, B. G.: Ultraviolet Spectra of Some Indole Derivatives, Including Tryptophan and Gramicidin. Arch. Biochem. Biophys. 21, 103–108 (1949)
Ellinger, A., and C. Flamand: Constitution of the Indole Group in Egg Albumin. IV. Preliminary Communication. Synthesis of Racernic Tryptophan. Bcr. 40, 3029–3033 (1907)
Elodi, P., and S. Lakatos: Anomalous Absorption of Tryptophan. Eur. J. Biochem. 36, 45–52 (1973)
EK, A., H. Kissman, J. B. Patrick, and B. Witkop: Chemical Contributions to the Mechanism of the Biological Oxidation ofTryntophan Fxnerientia 8,36–40 (1952)
Enfield, D. L., L. H. Ericsson, K. A. Walsh, H. Neurath. and K. Titani: Bovine Factor X1 (Stuart Factor). Primary Structure of the Light Chain. Proc. Natl. Acad. Sci. U.S. 72, 16–19 (1975)
Eskins, K., and M. Friedman: Photoaddition of Dimethyl Sulfoxide to Polypeptides. Photochem. Photobiol. 12, 245–247 (1970)
Evans, N. A.: Reaction of 3-methylindole with Singlet Oxygen. Aust. J. Chem. 24, 1971–1973 (1971)
Fahrenholz, F., H. Faulstich, and TH. Wieland: Components of the Green Deathcap Toadstool, Xvii; Peptide Syntheses, Xlviii. Synthesis of Norphalloin and of a Monocyclic Compound with 18-Membered Ring. Liebigs Ann. Chem. 743, 83–94 (1971)
Faulstich, H., Thh. Wieland, and C. JochHum: Über die Inhaltsstoffe des Grunen Knollenblatterpilzes. Xxxiv. Amanin und die Amanitine sind Sulfoxide. Liebigs Ann Che 713, 186–195 (1968)
Faulstych, H., E. Nebelin, and TH. Wielano: Peptide Syntheses, Liv. Syntheses of Analogs of Norphalloin. Liebigs Ann. Chem. 1973, 50–58.
Fasmman, G. D., and B. Bablouzian: Differential Spectrofluorometry, in: Methods in Enzymology - Enzyme Structure (C. H. W. Hirs and S. N. Timasheff, Eds.). 27, Part D, 811–822. London-New York: Academic Press. 1973
Finlayson, A. J.: Performic Acid Oxidation of Egg-white Lysozyme. Can. J. Biochem. 47. 31–37 (1969)
Foery, W., R. E. Mac Kenzie, F. Y. Wu, and D. B. MC Cormiere: Flavinyl Peptides. III. Studies of Intramolecular Interactions in Flavinyl Aromatic Amino Acids by Proton Magnetic Resonance. Biochemistry 9, 515–525 (1970)
Fontana, A.: Modification of Tryptophan with Bnps-Skatole (2-(2-Nitrophenylsulfenyl)-3-Methyl-3-Bromoindolenine), in: Enzyme Structure. Methods in Enzymology (C. H. W. Hirs and S. N. Timasheff, Eds.). 25, 419–423. New York: Academic Press. 1972
Fontana, A., and E. Gross: Solid Phase Synthesis of the Pentadecapeptide ValGramicidin A. Peptides 1972 (H. Hanson and H. D. Jakubke, Eds.). North Holland Publ. Co.. 229–234 (1972)
Fontana, A., F. Marchiiori, L. Moroder, and E. Scoffone: New Removal Conditions of Sulfenyl Group in Peptide Synthesis. Tetrahedron Letters 26, 2985–2987 (1966)
Fontana, A., F. Marchhiori, R. RocchIY, and P. Pajetta: On the Protection of the Amino Group by Sulfenyl Residues. I. Reaction of Tryptophan with Sulfenyl Halides. Gazz. Chim. Ital. 96, 1301–1312 (1966).
Fontana, A., and E. Scoffone: Sulfenyl Halides as Reagents in Peptide and Protein Chemistry. Mechanisms of Reactions of Sulfur Compounds (N. Kharasch, Ed.), Intra-Science Res. Foundation, Santa Monica, Calif. 4, 15–24 (1969)
Fontana, A., and E. Scoffone: Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins, in: Enzyme Structure. Methods in Enzymology (C. H. W. Hyrs and S. N. Timasheff, Eds.). 25, 482–494. New York: Academic Press. 1972
Fontana, A., and E. Scoffone: Degradation of Polypeptides and Proteins. Elucidation of Organic Structures by Physical and Chemical Methods (K. W. Bentley and G. W. Kirby, Eds.). 4 (II), 451–548. New York: J. Wiley. 1973
Fontana, A., E. Scoffone, and C. A. Benassi: Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins. II. Modification of Cysteinyl Residue. Biochemistry 7, 980–986 (1968)
Fontana, A., F. M. Veronese, and E. BoccÙ: Labelling of the Indole Nucleus of Tryptophan at the 2-Position. Acta Vitam. Enzymologica (Milan) 28, 79–83 (1975)
Fontana, A., C. Vita, and C. Toniolo: Selective Cleavage of the Single Tryptophanyl Peptide Bond in Horse Heart Cytochrome C. Febs Letters 32, 139–142 (1973)
Fontana, A.: unpublished results (1975).
FÖNY, W., R. E. MC Kenzie, F. Y. Wu, and D. B. MC Cormickk: Flavinyl reptioes. III. Studies of the Intramolecular Interactions in Flavinyl Aromatic Amino Acids by Proton Magnetic Resonance. Biochemistry 9, 515–525 (1970)
Foote, C. S.: Mechanisms of Photosensitized Oxidation. Science 162, 963–970 (1968)
Foote, C. S.: Photosensitized Oxygenation and the Role of Singlet Oxygen. Acc. Chem. Res. 1, 104–110 (1968)
Foote, C. S.: Ford-Hutchinson, A. W., and D. J. Perkins: Chemical Modification of the Tryptophan Groups of Transferrin. Eur. J. Biochem. 25, 415–419 (1972)
Fossel, E. T., W. R. Veatch, YU. A. Ovchinnnikov, and E. R. Blout: A C13 Nuclear Magnetic Resonance Study of Gramicidin A in Monomer and Dimer Films. Biochemistry 13, 5264–5275 (1974)
Friedman, M., and J. W. Finley: Methods of Tryptophan Analysis. Agr. Food Chem. 19, 626–631 (1971)
Friedman, M., L. H. Krull, and J. F. Cavins: Reactions of Amino Acids, Peptides and Proteins with α,β-unsaturated Compounds. Xiv. Chromatographic Determination of Cystine and Cysteine Residues in Proteins as S-β-(4-pyridylethyl)cysteine. J. Biol. Chem. 245, 3868–3871 (1970)
Fukul, K., T. Yonezawa, C. Nagata, and H. SHiNgu: Molecular Orbital Theory of Orientation in Aromatic, Heteroaromatic and Other Conjugated Molecules. J. Chem. Phys. 22. 1433–1442 (1954).
Gabriel, M., D. Larchier, H. Rinnert, and C. Thirion: Magnetic Circular Dichroism of Tyrosine and Tryptophan. Variation as a Function of pH. C. R. Acad. Sci Ser R 276, 39–41 (1973)
Gaitonde, M. K., and T. Dovey: A Rapid and Direct Method for the Quantitative Determination of Tryptophan in the Intact Protein. Biochem. J. 117, 907–911 (1 970
Gaitonde, M. K.: A Fluorimetric Method for the Determination of Tryptophan in Animal Tissues Biochem J 139 625–631 (1974)
Gartland, G. L., G. R. Freeman, and C. E. Bugg: Crystal Structures of Tryptamine Picrate and D,L-Tryptophan Picrate-Methanol, Two Indole Donor-Acceptor Complexes. Acta Cryst. B 30, 1841–1849 (1974)
Gehrke, C. W., and H. Takeda: Gas-Liquid Chromatographic Analysis of Tryptophan in Proteins. J. Chromat. 76, 77–89 (1973)
Geiger, R., K. Sturm, and W. Siedel: Synthesis of a Biologically Active Tricosapeptide Amide with the Amino Acid Sequence 1–23 of Corticotropin (Acth). Ber. 97, 1207–1213 (1964)
Geiger, R., W. Konig, H. Wissmann, K. Geisen, and F. Enzmann: Synthesis and Characterisation of a Decapeptide Having LH-RH/Fsh-RH Activity. Biochem. Biophys. Res. Commun. 45, 767–773 (1971).
Geric, J. T. C., and R. A. Rimerman: N-Formyl-L-Tryptophan – Chymotrypsin Complex in Solution. Biochem. Biophys. Res. Commun. 40. 1149–1154 (1970)
Glazer, A. N.: Specific Chemical Modification of Proteins. Ann. Rev. Biochem. 39 101–130 (1970)
Glickson, J. D., C. C. Mc Donald, and W. D. Phillips: Assignment of Tryptophan Indole NH Proton Resonance of Lysozyme. Biochem. Biophys. Res. Commun. 35, 492–498 (1969)
Gomyo, T., and M. Fujimaki: Changes of Protein by Dye-sensitized Photooxidation. III. Photodecomposition Products of Lysozyme. Agric. Biol. Chem. Tokyo 34, 302–309 (1970)
Goodman, M., and C. ToNiolo: Conformational Studies of Proteins with Aromatic Side Chain Effects. Bi0p0lymers 6. 1673–1689 (1968)
Goodwin, T. W., and R. A. Morton: Spectrophotometric Determinations of Tyrosine and Tryptophan in Proteins. Biochem. J. 40, 628–632 (1946)
Gosztonyi, T., J. Marton, and A. Kovacs: The Labeling of β-lipoprotein with Tritium. Nature (London) 208, 381–382 (1965)
Goswami, A. K.: Determination of Tryptophan and Indole Substances by a Colorimetric Diazotisation Method. Analyst 99, 657–660 (1974)
Green, N. M., and B. Witkop: Oxidation Studies of Indoles and the Tertiary Structure of Proteins. Trans. N. Y. Acad. Sci. 26, 659–669 (1964)
Green, J. P., and J. P. Mabrien: Quantum Chemical Studies of Charge Transfer Complexes of Indoles. Proc. Natl. Acad. Sci. U.S.A. 54, 659–664 (1965)
Green, N. M., and M. D. Melamed: Optical Rotatory Dispersion, Circular Dichroism and Far-Ultraviolet Spectra of Avidin and Streptavidin. J. Biochem. 100, 614–621 (1966)
Greenstein, J. P., and M. Winitz: Chemistry of the Amino Acids 3, 2316–2347. New York: J. Wiley. 1961
Gruen, L. C.: Effect of other Amino Acids on Recovery of Tryptophan Following Acid Hydrolysis. Aust. J. Biol. Sci. 26, 287–290 (1973)
Gruen, L. C., and P. W. Nicholls: Improved Recovery of Tryptophan Following Acid Hydrolysis of Proteins. Anal. Biochem. 47, 348–355 (1972)
Gurnani, S., M. Arifuddin, and K. T. Augusti: Effect of Visible Light on Amino Acids. I. Tryptophan. Photochem. Photobiol. 5, 495–505 (1966)
Hachimori, Y., H. Horinishi, K. Kurihara, and K. Shibata: States of Amino Acid Residues in Proteins. V. Different Reactivities with H2O2 of Tryptophan Residues in Lysozyme, Proteinases, and Zymogens. Biochim. Biophys. Acta 93, 346–360 (1964)
Hachimori, Y., K. Kurihara, H. Horinishi, A. Matsushima, and K. Shibata: States of Amino Acid Residues in Proteins. Viii. Tyrosine, Histidine, and Tryptophan Residues in Chymotrypsin in the Presence of Substrate and in Diisopropylphosphorylchymotrypsin. Biochim. Biophys. Acta 105, 167–177 (1965)
Hartdegen, F. J., and J. A. Rupley: Inactivation of Lysozyme by Iodine. Oxidation of a Single Tryptophan. Biochim. Biophys. Acta 92, 625–627 (1964)
Hartdegen, F. J., and J. A. Rupley: Oxidation ot Lysozyme by Iodine: laentification of Oxindolylalanine 108. J. Mol. Biol. 80, 649–656 (1973)
Hayaishi, O., S. Rothberg, A. H. Metler, and Y. Saito: Studies on Oxygenases. Enzymatic Formation of Kynurenine from Tryptophan. J. Biol. Chem. 229, 889–896 (1957)
Hayaishi, O.: Enzyme Hydroxylation. Ann. Rev. Biochem. 38, 21–44 (1969)
Heber, H., H. Faulstich, and 1H. Wieland: Syntheses of Furtner Analogues of Norphalloin. Gly1-, L-Val1- and D-Abu2-Norphalloin and (β-Trideutero)-Ala5Norphalloin. Intern. J. Peptide Protein Res. 6, 381–389 (1974)
Heinrichi, C. P., K. Noack, and O. Wiss: Chemical Modification of Tryptophan at the Binding Site of Thiamine Pyrophosphate in Transketolase from Baker’s Yeast. Biochem. Biophys. Res. Commun. 49, 1427–1432 (1972)
Heinrich, C. P., S. Adam, and W. Arnold: The Reaction of Dimethyl (2-Hydroxy5-Nitrobenzyl) Sulfonium Bromide with N-Acetyl-L-Tryptophan Amide. Febs Lett. 33, 181–183 (1973)
Heinrikson, R. L., and K. J. Kramer: Recent Advances in the Chemical Modification and Covalent Structural Analysis of Proteins, in: Progress in Biorganic Chemistry (E. T. Kaiser and F. J. KÉzDY, Eds.), p. 141–250. New York: J. Wiley. 1974
Helene, C., J. L. Dimicoli, H. N. Borazan, M. Durand, J. C. Maurizot, and J. J. Taulme: in: Conformation of Biological Molecules and Polymers. Interactions of Aromatic Amino Acids with Nucleic Acids (E. D. Bergmann and B. Pullmann, Eds.), 361–380. Jerusalem: The Israel Academy of Sciences and Humanities. 1973
Hermodson, M. A., L. H. Ericsson, H. Neurath, and K. A. Walsh: Determination of the Amino Acid Sequence of Porcine Trypsin by Sequenator Analysis. Biochemistry 12, 3146–3153 (1973)
Herskovits, T. T.: Difference Spectroscopy in Methods in Enzymology, Enzyme Structure (C. H. W. Hirs, Ed.) 11, 748–775. London-New York: Academic Press. 1967
Hidenari, Y., F. Morita, and K. Yagi: Interaction of Heavy Meromyosin from Substrate. VI. Difference Absorption Spectra Induced by Atp Analogs and Chemical Modification of Tryptophanyl Residue with 2-hydroxy-5-nitrobenzyl Bromide. J. Biochem. (Tokyo) 72, 1227–1236 (1972)
Hill, R. L., and W. R. Schmidt: Complete Enzymic Hydrolysis of Proteins. J. Biol. Chem. 237, 389–396 (1962)
Hinnan, R. L., and C. P. Baumann: Reactions of N-Bromosuccinimide and Indoles. A Simple Synthesis of 3-Bromo-oxindoles. J. Org. Chem. 29, 1206–1215 (1964)
Hinman, L. M., C. R. Coan, and D. A. Deranleau: Solution Topography of Proteins by Charge Transfer. Model Complexes, Ribonuclease, and Lysozyme. J. Amer. Chem. Soc. 96, 7067–7073 (1974)
Hino, T., and M. Nakagawa: 1-(3-Methyl-2-Indolyl) Pyridinium Bromide. Synthesis and Autoxidation of its Catalytic Hydrogenation Product. Tetrahedron 23, 1441–1450 (1967)
Hino, T., M. Nakagawa, and S. Akaboshi: 2-Ethoxyindoles and 2-Ethylthioindoles: Their Autoxidation and Reactions with Piperidine. J. C. S. Chem. Commun. 656–658 (1967)
Hino, T., and M. Nakagawa: Oxidation-Reduction of 2-Substituted 3-Benzylindoles and 3-Benzylidene-3 H-indoles. Model Reactions for Alcohol Dehydrogenase. J. Amer. Chem. Soc. 91, 4598–4599 (1969)
Hino, T., H. Yamaguchi, and M. Nakagawa: Oxidation of 2-Ethylthioindoles with Hydrogen Peroxide. Oxidative Migration of the Ethylsulphinyl Group. J. C. S. Chem. Commun. 473–474 (1972)
HiRoshi, O.: Microbial Formation of L-Tryptophan from D-Tryptophan. Agr. Biol. Chem. 32, 254–256 (1968).
Hirs, C. H. W.: Performic Acid Oxidation, in: Methods in Enzymology (C. H. W. Hirs, Ed.) 11, 197–199. London-New York: Academic Press. 1967
Hirs, C. H. W.: Methods in Enzymology 11. London-New York: Academic Press. 1967.
Hofmann, K., J. A. Montibeller, and F. M. Finn: Acth Antagonists. Proc. Natl. Acad. Sci. U.S. 71, 80–83 (1974)
Holiday, E. R.: Spectrophotometry of Proteins. I. Absorption Spectra of Tyrosine, Tryptophan and Their Mixtures. Biochem. J. 30, 1795–1799 (1936)
Holladay, L. A., R. G. Hammonds, JR., and D. Puett: Growth Hormone Conformation and Conformational Eauilibria. Biochemistry 13, 1653–1661 (1974) , ,.
Holmgren, A.: Reversible Chemical Modification of the Tryptophan Residues of Thioredoxin from Escherichia coli B. Eur. J. Biochem. 26, 528–534 (1972)
Holmgren, A.: Tryptophan Fluorescence Study of Conformational Transition of the Oxidized and Reduced Form of Thioredoxin. J. Biol. Chem. 247, 1992–1998 (1972)
Effects of Oxidation of Tryptophan Residues in Thioredoxin from Escherichia coli by N-Bromosuccinimide. J. Biol. Chem. 248, 4106–4111 (1973)
Holmquist, B., and B. L. Vallee: Tryptophan Quantitation by Magnetic Circular Dichroism in Native and Modified Proteins. Biochemistry 12, 4409–4417 (1973)
Holt, L. A., B. Milligan, and D. F. Rivett: Tritiation of Tryptophyl Residues in Proteins. Biochemistry 10, 3559–3564 (1971)
Holt, L. A., and B. Milligan: Application of Enzymic Hydrolysis and Tritium Labelling to a Study of the Modification of Tryptophyl Residues in Proteins. Aust. J. Biol. Sci. 26, 871–876 (1973)
Horton, H. R., and D. E. Koshland, JR.: Environmentally Sensitive Groups Attached to Proteins, in: Methods in Enzymology (C. H. W. Hirs, Ed.) 11, 856–870. London-New York: Academic Press. 1967
Horton, H. R., and D. E. Koshland, JR.: Modification of Proteins with Active Benzyl Halides, in: Methods in Enzymology (C. H. W. Hirs and S. N. TiMasheff, Eds.) 11, 468–482. London-New York: Academic Press. 1972
Horton, H. R., and G. Young: 2-Acetoxy-5-nitrobenzyl Chloride. A Reagent Designed to Introduce a Reporter Group Near the Active Site of Chymotrypsin. Biochim. Biophys. Acta 194, 272–278 (1969)
Horton, H. R., and W. P. Tucker: Dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium Salts. Water Soluble Environmentally Sensitive Protein Reagents. J. Biol. Chem. 245, 3397–3401 (1970)
Hugli, T. E., and S. Moore: Determination of the Tryptophan Content of Proteins by Ion Exchange Chromatography of Alkaline Hydrolysates. J. Biol. Chem. 247, 2828–2834 (1972)
Ikeda, K., and K. Hamaguchi: Binding of N1-Methylnicotinamide Chloride to Trp-62 Linked with the Ionization of Glu-35 of Hen Egg-white Lysozyme. J. Biochem. (Tokyo) 74, 221–230 (1973)
Imoto, T., F. J. Hartdegen, and J. A. Rupley: Oxidation of Lysozyme by Iodine: Isolation of an Inactive Product and its Conversion to an Oxindolealanine-Lysozyme. J. Mol. Biol. 80, 637–648 (1973)
Imoto, T., and J. A. Rupley: Oxidation of Lysozyme by Iodine: Identification and Properties of an Oxindolyl Ester Intermediate: Evidence for Participation of Glutamic Acid 35 in Catalysis. J. Mol. Biol. 80. 657–667 (1973)
Inoue, M., and H. Hayatsu: Interactions between Bisulfite and Amino Acids. Formation of Methionine Sulfoxide from Methionine in the Presence of Oxygen. Chem. Pharm. Bull. 19, 1286–1289 (1971)
IRiE, M.: State of Tryptophan Residue in Ribonuclease T1 and Carboxymethyl Ribonuclease T1. J. Biochem. 68. 31–37 (1970)
Irie, M., M. Harada, and F. Sawada: State of Tryptophan Residues in Ribonuclease from Aspergillus Saitoi. J. Biochem. 72, 1351–1359 (1972)
Isbell, B. E., C. Rice-Evans, and G. H. Beaven: The Conformation of Gramicidin A in Solution. Febs Letters 25, 192–196 (1972)
Jacobsen, C.: Chemical Modification of the High-Affinity Bilirubin Binding Site of Human Serum Albumin. Eur. J. Biochem. 27, 513–519 (1972)
Jayson, G. G., G. Scholes, and J. Weiss: Formation of Formylkynurenine by the Action of X-Rays on Tryptophan in Aqueous Solution. Biochem. J. 57, 386–390 (1954)
Jackson, A. H., B. Naidor, and P. Smitgh: Electrophilic Substitution in Indoles. IV. The Cyclization of Indolyl-butanole to Tetrahydrocarbazole. Tetrahedron 24, 6119–6129 (1968)
Jackson, A. H., and A. E. Smith: Electrophilic Substitution in Indoles. I. Model Experiments Related to the Synthesis of Echinulin. Tetrahedron 21, 989–1000 (1965)
Jerina, D. M., J. W. Daly, B. Witkop, P. Zaltzman-Niremberg, and S. Udenfriend: The Role of Arene Oxide-Oxepin System in the Metabolism of Aromatic Substrates. Formation of 1,2-Naphthalene Oxide from Naphthalene by Liver Microsomes. J. Amer. Chem. Soc. 90, 6525–6527 (1968)
Jorkasky, D. K., S. E. Pearson, and C. L. Borders, Jr.: Reversible Inactivation of Avian Lysozymes by Dimethyl (2-Hydroxy-5-Nitrobenzyl)-Sulfonium Bromide. Biochem. Biophys. Res. Commun. 52, 987–991 (1973)
Jori, G., M. FoliN, G. Gennari, G. Galiazzo, and O. BUso: Photooxidation of Lanthanide Ion-Lysozyme Complexes. A New Approach to the Evaluation of Intramolecular Distances in Proteins. Photochem. Photobiol. 19, 419–434 (1974)
Jori, G., and G. Galiazzo: Proflavine-Sensitized Selective Photooxidation of the Tryptophyl Residues in Papain. Photochem. Photobiol. 14, 607–619 (1971) and references therein.
Jori, G., and G. Galiazzo: The Contribution of the Single Tryptophyl Residues to the Fluorescence Emission of Porcine Elastase. Z. Naturforsch. 29b, 261–265 (1974)
JoRI, G., G. Galiazzo, and O. BUsO: Photosensitized Oxidation of Elastase. Selective Modification of the Tryptophyl Residues. Arch. Biochem. Biophys. 158, 116–125 (1973)
JoRI, G., G. Galiazzo, and G. Gennari: Photosensitized Conversion of Tryptophan to β-carboline Derivatives. Photochem. Photobiol. 9, 179–181 (1969)
Jorkasky, D. K., S. E. Pearson, and C. L. Borders: Reversible Inactivation of Avian Lysozymes by Dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium Bromide. Biochem. Biophys. Res. Commun. 52, 987–991 (1973)
Julian, P. L., E. W. Meyer, and H. C. Printy: The Chemistry of Indoles, in Heterocyclic Compounds (R. C. Elderfield) 3, 1–271. New York: J. Wiley. 1952
Julian, P. L., E. E. Dailey, H. C. Printy, H. L. Cohen, and S. Hamashige: Studies in the Indole. Series Xvi. Oxindole-3-alanine and Dioxindole-3-alanine. J. Amer. Chem. Soc. 78, 3503–3508 (1956)
Juneja, K. K., A. D. Sule, and V. B. Chipalkatti: Estimation of Tryptophan Content of Wool by the Barium Hydroxide Hydrolysis Method. Text. Res. J. 38, 461–466 (1968)
Kanaoka, Y., E. Sato, and O. Yonemitsu: Amino Acids and Peptides. 11. Cyclodehydration of Some Tryptophan-Dipeptides and their Derivatives with Polyphosphate Ester. Tetrahedron 24, 2591–2594 (1968)
Kantouch, A. A., and A. Bendak: Action of Periodic Acid and its Salts on Wool. II. Amino Acids in Periodate-oxidized Wool. Text. Res. J. 39, 851–858 (1969)
Katrukha, G. S., N. Zylber, and V. Keil-Dlouha: Influence of the Substitution of Tryptophan-215 in Bovine Chymotrypsinogen A on its Potential Enzymic Activity. Febs Lett. 29, 25–30 (1973)
Kawauchi, H., T. A. Bewley, and C. H. LI: Selective Modification of Tryptophan149 in Ovine Pituitary Lactogenic Hormone. Biochemistry 12, 2124–2130 (1973)
Kearns, D. R.: Physical Chemical Properties of Singlet Molecular Oxygen. Chem. Reviews 71, 395–427 (1971).
Kirby, G. W., and M. J. Varley: Synthesis of Tryptophan Stereoselectively Labelled with Tritium and Deuterium in the β-Methylene Group; the Steric Course of Hydroxylation in Sporidesmin Biosynthesis. J. C. S. Chem. Comm. 833–834 (1974)
Kobayashi, T., and N. Inokuchi: A New Method for the Preparation of Oxindoles from Parent Indoles. Tetrahedron 20, 2055–2058 (1964)
Komachiya, Y., S. Suzuki, T. Yamada, H. Miyayashiki, and S. Sakurai: Dltryptophan. Nippon Kagaki Zasshi 86, 856–860 (1965)
Korte, K., and U. Schmidt: Syntheses in the Adermine Series IV. Mechanism of the Cysteine and Tryptophan Biosynthesis. Monatsh. Chem. 102, 207–213 (1971)
Kravchenko, N. A., and V. K. Lapuk: Isolation and Characteristics of the Products of Selective Photooxidation of Lysozyme Through Tryptophan. Biokhimiya 34, 832–838 (1969)
Kronman, M. J., and F. M. Robbins: Buried and Exposed Groups in Proteins, in: Fine Structure of Proteins and Nucleic Acids (G. D. Fasman and S. N. Timasheff, Eds.), Marcel Dekker 1970, 271–408.
Kronman, M. J., F. M. Robbins, and R. E. Andreotti: Reaction of N-Bromosuccinimide with Lysozyme. Biochim. Biophys. Acta 147, 462–472 (1967)
Lapuk, V. K., L. A. Chistyakora, and N. A. Kravchenko: Tryptophan Determination in Lysozyme and its Photooxidation Products. Anal. Biochem. 24, 80–89 (1968)
Liu, T.-Y.: Determination of Tryptophan, in: Methods in Enzymology (C. H. W. Hirs and S. N. Timasheff, Eds.) 25, 44–55, London-New York: Academic Press. 1972
Liu, T. Y., and Y. H. Chang: Hydrolysis of Proteins with p-Toluenesulfonic Acid. Determination of Tryptophan. J. Biol. Chem. 246, 2842–2848 (1971)
Liudskog, S., and H. Nilsson: Location of Tryptophanyl Groups in Human and Bovine Carbonic Anhydrases. Ultraviolet Difference Spectra and Chemical Modification. Biochim. Biophys. Acta 295, 117–130 (1973)
Loudon, G. M., and D. E. Kohsland, JR.: Chemistry of a Reporter Group: 2-Hydroxy-5-nitrobenzyl Bromide. J. Biol. Chem. 245, 2247–2254 (1970)
Lowe, G., and A. S. Whitworth: A Kinetic and Fluorimetric Investigation of Papain Modified at Tryptophan-69 and -177 by N-Bromosuccinimide. Biochem. J. 141, 503–515 (1974)
Maeda, I., and R. Yoshida: The Reaction Products of the Hydroformylation of Acrolein Acetals and Acetates. Bull. Chem. Soc. Japan 41, 2969–2974 (1968)
Maeda, I., and R. Yoshida: Synthesis of DL-Tryptophan from Acrolein. Bull. Chem. Soc. Japan 41, 2975–2978 (1968)
Maeda, H., and J. Meienhofer: On the Tryptophan Content of Neocarzinostatin. Int. J. Protein Res. 2, 135–136 (1970)
Maeda, H.: Chemical Reactivity and State of Tryptophan Residues in Neocarzinostatin under Physiological Conditions. J. Antibiot. 26, 776–777 (1973)
Maeda, K., T. Mishima, and T. Hagachi: The Formation of Substituted Quinazolines from Substituted Indoles by the Sensitized Photo-oxygenation in the Presence of Ammonium Acetate. Bull. Chem. Soc. Japan 47, 334–338 (1974)
Maigret, B., B. Pullman, and D. Perahia: Molecular Orbital Calculations of the Conformation of Polypeptides and Proteins. II. Conformational Energy Maps and Stereochemical Rotational States of Aromatic Residues. Biopolymers 10, 107–128 (1971).
Mandel, M.: Proton Magnetic Resonance Spectra of Some Proteins. I. Ribonuclease, Oxidized Ribonuclease, Lysozyme and Cytochrome C. J. Biol. Chem. 240, 1586–1592 (1965)
Mann, S.: Quinazoline Derivatives in Pseudomonas Aeruginosa. Arch. Mikrobiol. 56, 324–329 (1967)
Marche, P., J.-P. Girma, J.-L. Morgat, and P. Fromageot: Specific Tritiation of Indole Derivatives by Catalytic Desulfenylation. Application to the Labelling of Tryptophan Containing Peptides. Eur. J. Biochem. 50, 375–382 (1975)
Marche, P., J. L. Morgat, and P. Fromageot: Solvent Effects on Luteinizingand Follicle-Stimulating-Hormone Releasing Factor. Polymorphism Studied by Circular Dichroism. Eur. J. Biochem. 40, 513–518 (1973).
Marshall, G. R.: Studies with Tryptophan in Solid-Phase Synthesis. In: Adv. Exp. Med. Biol. (N. Back, L. Martini, and R. Paoletti, Eds.), II, Pharmacology of Hormonal Polypeptides and Proteins, 48–58. New York: Plenum Press. 1968
Matsubara, H., and R. M. Sasakc. High Recovery of Tryptophan from Acid Hydrolyzates of Proteins. Biochem. Biophys. Res. Commun. 35, 175–181 (1969)
Matsunaga, Y.: Charge-Transfer and Proton-Transfer in the Formation of Molecular Complexes. V. Tryptophan Picrate. Bull. Chem. Soc. Japan. 46, 998–999 (1973)
Matsuo, H., A. Arimura, R. M. G. Nair, and A. V. Schally: Synthesis of the Porcine LH- and Fsh-releasing Hormone by the Solid-phase Method. Biochem. Biophys. Res. Commun. 45, 822–827 (1971)
MC Donald, C. C., and W. D. Phillips: Proton Magnetic Resonance Studies of Horse Cytochrome c. Biochemistry 12, 3170–3186 (1973)
MC Farland, G., B. Y. Inoue, and K. Nakanishi: The Reaction of Koshland’s Protein Reagent with Tryptophan. Tetrahedron Letters 857–860 (1969)
MC Farland, T. M., and J. E. COlEman: Magnetic Circular Dichroism of Tryptophanyl Residues in Proteins. Azurin and Carbonic Anhydrase. Eur. J. Biochem. 29, 521–527 (1972)
Mclaren, A. D.: Photochemistry of Enzymes, Proteins and Viruses. Adv. Enzymology 9, 75–170 (1969)
Mclean, S., and G. I. Dimitrienko: Autooxidation of 2,3-Dialkylindoles. Can. J. Chem. 49, 3642–3647 (1971)
Merrifield, R. B.: Solid-phase Peptide Synthesis. Adv. in Enzymology 32, 221–296 (1969)
Messineo, L., and E. Musarra: A Sensitive Spectrophotometric Method for the Determination of Free or Bound Tryptophan. Intern. J. Biochem. 3, 700–704 (1972)
Mingoia, Q.: On Arsenical Derivatives of Pyrrole and Indole. Gazz. Chim. Ital. 60, 134–140 (1930)
Mole, J. E., and H. R. Horton: 2-Chloromethyl-4-nitrophenyl (N-Carbobenzoxy) glycinate. A New Reagent Designed to Introduce an Environmentally Sensitive Conformational Probe near the Active Site of Papain. Biochemistry 12, 5278–5285 (1973)
Monahan, M. W., and J. Rivier: Luteinizing Hormone Releasing Factor. The Total Solid-phase Synthesis on a Benzhydrylamine Polymer. Biochem. Biophys. Res. Commun. 48, 1100–1105 (1972)
Mondino, A., and G. Bongiovanni : Experimental Study of Amino Acid Degradation Under Open Flask Hydrolytic Conditions. J. Chromat. 52, 405–413 (1970)
Moon, K., and E. L. Smith: Sequence of Bovine Liver Glutamate Dehydrogenase. III. Peptides Produced by Specific Chemical Cleavages; the Complete Sequence of the Protein. J. Biol. Chem. 238, 3082–3088 (1973)
Morihara, K., and K. Nagami: Tryptophan Residue in the Active Site of Papain. J. Biochem. (Tokyo) 65, 321–323 (1969)
Morishita, M., and F. Sakkiyama: The non-enzymatic Cleavage of Peptide Bonds. H. The Chemical Cleavage of the Tryptophyl Bond in Several Synthetic Peptides. Bull. Chem. Soc. Japan 43, 524–530 (1970)
Morishita, M., F. Sakiyama, and K. Narita: The Chemical Cleavage of the Tryptophyl Bond. Bull. Chem. Soc. Japan 40, 433–435 (1967)
Morley, J. S.: Polypeptides. Part IV. Synthesis of Human Gastrin (HI). J. Chem. Soc. c 22, 2410–2421 (1967)
Moroder, L., G. Borin, F. Marchiori, and E. Scoffone: Synthetic Peptides Related to the Entire Sequence of Yeast Iso-l-cytochrome c. Biopolymers 11, 2191–2194 (1972).
Morris, A. J., A. J. Geddes, and B. Sheldrick: Cyclo-glycyl-tryptophyl, C13H13N3O2. Cryst. Struct. Commun. 3, 345–349 (1974)
Mulvey, R. S., and S. Beychok: Further Studies on the Circular Dichroism of Human Lysozyme. Implications for Structure and Comparison of Predicted Secondary Structures in Homologous Lysozymes. Biochemistry 13, 2980–2985 (1974)
Myer, Y. P., and L. H. Macdonald: The Circular Dichroism of L-Tryptophan by an Improved Dichrograph. J. Amer. Chem. Soc. 89, 7142–7144 (1967)
Myer, Y. P., and P. K. Pal: Conformation of Cytochromes. Viii. Spectroscopic Properties of N-Bromosuccinimide-modified Horse Heart Cytochrome C. Biochemistry 11, 4205–4216 (1972)
Nakagawa, M., and T. Hino: 2-Ethoxy and 2-Ethylthioindoles. Autoxidation and Nucleophilic Substitutions. Tetrahedron 26, 4491–4503 (1970)
Nakagawa, M., T. Kaneko, H. Yamagughi, T. Kawashima, and T. Hino: Photoinduced Oxygenation of Tryptamines by Aromatic Amine N-Oxides. Tetrahedron 30, 2591–2600 (1974)
Nakagawa, M., T. Kaneko, K. Yoshikawa, and T. Hino: Photosensitized Oxygenation of Tryptophan Methyl Ester and Nb-Methyltryptamine. Isolation and Identi fication of 3a-Hydroxypyrroloindole and 4a-Hydroxy-1,2-oxazinoindole. J. Amer. Chem. Soc. 96, 624–625 (1974)
Nakagawa, M., H. Yamaguchi, and T. Hino: Autoxidation of Indoles Having a Hetero-Atom at 2-Position. Decomposition of the Intermediate 3-Hydroperoxide. Tetrahedron Letters 47, 4035–4038 (1970)
Nakamura, A., and O. Jardetzky: Systematic Analysis of Chemical Shifts in the Nuclear Magnetic Resonance Spectra of Peptide Chains. I. Glycine-Containing Peptides. Proc. Nat. Acad. Sci. U.S. 58, 2212–2219 (1967)
Nedkov, P., and B. Meloun: Modification of Tryptophan and Tyrosine Residues of Dolphin Myoglobin. Collect. Czech. Chem. Commun. 34, 2021–2029 (1969)
Neumann, N. P.: Oxidation with Hydrogen Peroxide, in: Methods in Enzymology (C. H. W. Hirs and S. N. Timasheff, Eds.) 25, 393–401. New York: Academic Press. 1972
Norman, R. O. C., and R. Taylor: Electrophilic Substitution in Benzenoid Compounds, p.282. Amsterdam: Elsevier. 1965
Oelshlegel, F. J., JR., J. R. Schroeder, and M. A. Stahmann: Simple Procedure for Basic Hydrolysis of Proteins and Rapid Determination of Tryptophan Using a Starch Column. Anal. Biochem. 34, 331–337 (1970)
O’Hern, D. J., P. K. Pal, and Y. P. Myer: Conformational and Functional Studies of Chemically Modified Cytochromes: N-Bromosuccinimide- and Formyl-Cytochromes C. Biochemistry 14, 382–391 (1975)
Ohno, M.: personal communication, reported in ref. [124].
Ohno, M., T. F. Spande, and B. Witkop: Cyclization of Tryptophan and Tryptamine Derivatives to 2,3-Dihydropyrrolo [2,3-b] indoles. J. Amer. Chem. Soc. 92, 343–348 (1970)
Ohno, M., T. F. Spande, and B. Witkop: A New Practical Synthesis of L-2-Hydroxytryptophan and Its Derivatives. J. Org. Chem. 39, 2635–2637 (1974)
Ohno, M., S. Tsukamoto, S. Sato, and N. Izumiya: Improved Solid-Phase Synthesis of Tryptophan-Containing Peptides. 11. Use of N’-t-Butyloxycarbonyl-N’formyltryptophan. Bull. Chem. Soc. Japan. 46, 3280–3285 (1973)
Olcott, H. S., and H. Fraenkel-Conrat: Formation and Loss of Cysteine During Acid Hydrolysis of Proteins. Role of Tryptophan. J. Biol. Chem. 171, 583–594 (1947)
Oldfield, E., and A. Allerhand: Identification of Tryptophan Resonance in Natural Abundance Carbon-13 Nuclear Magnetic Resonance Spectra of Proteins. Application of Partially Relaxed Fourier Trasform Spectroscopy. J. Amer. Chem. Soc. 97, 221–224 (1975)
Omenn, G. S., A. Fontana, and C. B. Anfinsen: Modification of the Single Tryptophan Residue in Staphylococcal Nuclease by a New Mild Oxidizing Agent. J. Biol. Chem. 245, 1895–1902 (1970)
Omenn, G. S., and I. Parikh: Modification of Staphylococcal Nuclease with Nitrophenylsulfenyl Halides. Biochemistry 10, 1173–1177 (1971)
Ottenheym, J. H.: Status and Prospects for Amino Acid Production by Chemical Synthesis, in: Amino Acid Fortification Protein Foods, Rep. Intern. Conf. 2, 449–466 (1969)
Overby, L. R.: Reciprocal Resolution of DL-tryptophan and DL-α-phenylethylamine. J. Org. Chem. 23, 1393–1394 (1958)
Pailthope, M. T., and C. H. Nicholls: Indole Nitrogen-Hydrogen Bond Fission During the Photolysis of Tryptophan. Photochem. Photobiol. 14, 135–145 (1971)
Pasternak, R. A.: The Crystal Structure of Glycyl-L-Tryptophan Dihydrate. Acta Cryst. 9, 341–349 (1956)
Patchornik, A., W. B. Lawson, E. Gross, and B. Witkop: The Use of N- Bromosuccinimide and N-Bromoacctamide for the Selective Cleavage of C-Tryptophyl Peptide Bonds in Model Peptides and Glucagon. J. Amer. Chem. Soc. 82, 5923–5927 (1960)
Patel, D. J., L. Kampa, R. G. Shulman, T. Yamane, and B. J. Wyluda: Proton Nuclear Magnetic Resonance Studies of Myoglobin in Water. Proc. Nat. Acad. Sci. U.S. 67, 1109–1115 (1970)
Peggion, E., A. Cosani, A. S. Verdini, A. Del Pra, and M. Mammi: Conformational Studies on Poly-L-Tryptophan: Circular Dichroism and X-Ray Diffraction Studies. Biopolymers 6, 1477 1486 (1968)
Peggion, E., A. Fontana, and A. Cosani: Conformational Studies on a Modified Poly-L-Tryptophan: Circular Dichroism and Optical Rotatory Dispersion of Poly2-(2-nitrophenylsulfenyl)-L-tryptophan and of Random Copolymers of L-Tryptophan and 2-(2-Nitrophenylsulfeny1)-L-tryptophan. Biopolymers 7, 517–526 (1969)
Penke, B., R. Ferenczi, and K. Kovacs: A New Acid Hydrolysis Method for Determining Tryptophan in Peptides and Proteins. Anal. Biochem. 60, 45–50 (1974)
Peter, G., and B. Rajewsky: The Indirect Action of X-Rays on Amino Acids. II. Irradiation of Tryptophan. Z. Naturforsch. 18b, 110–114 (1969)
Pfaender, P., G. Feige, and TH. Wieland: Indole zum Vergleich mit AmanitaGiften. VI. Hydroxylierung von Tryptophan und Tryptophyl-peptiden. Z. Naturforsch. 23b, 926–930 (1968)
Phillips, D. C.: The Hen Egg-white Lysozyme Molecule. Proc. Nat. Acad. Sci. U.S. 57, 484–495 (1967)
Pirie, A.: Formation of N’-Formylkynuremine in Proteins from Lens and Other Sources by Exposure to Sunlight. Biochem. J. 125, 203–208 (1971)
Pirie, A., and K. J. Dilley: Photo-Oxidation of N’-Formylkynurenine and Tryptophan Peptides by Sunlight or Simulated Sunlight. Photochem. Photobiol. 19, 115–118 (1974)
Pisano, J. J.: Gas-Liquid Chromatography (Glc) of Amino Acid Derivatives, in: Methods in Enzymology (C. H. W. Hirs and S. N. Timashefe, Eds.) 25, 27–44. London-New York: Academic Press. 1972
Previero, A., and E. Bordignon: Controlled Modification of Tryptophan, Methionine, Cystine and Tyrosine in Peptides and Proteins. Gazz. Chim. Ital. 94, 630–638 (1964)
Previero, A., M. A. Coletti, and L. Galzigna: Modification of Tryptophan Residues in Trypsin, α-Chymotrypsin and Pepsinogen. Biochem. Biophys. Res. Commun. 16, 195–198 (1964)
Previero, A., M. A. Coletti-Previero, and P. JolliÈS: Nonenzymic Cleavage of Tryptophyl Peptide Bonds in Peptides and Proteins. II. Release of a Chemically Modified Tryptophan Residue from Model Peptides by a Mild Basic Treatment. Biochim. Biophys. Acta 124, 400–402 (1966)
Previero, A., M. A. Coletti-Previero, and P. JolliÈS: Localization of Non-Essential Tryptophan Residues for the Biological Activity of Lysozyme. J. Mol. Biol. 24, 261–268 (1967)
Previero, A., M. A. Coletti-Previero, and J. C. Cavadore: A Reversible Chemical Modification of the Tryptophan Residue. Biochim. Biophys. Acta 147, 453–461 (1967)
Previero, A., M. A. Coletti-Previero, and P. JollÈS: Nonenzymatic Cleavage of Tryptophyl Peptide Bonds in Peptides and Proteins. I. Cleavage of C-tryptophyl Peptide Bonds in Model Peptides through their Conversion into N-Formylkynurenine Derivatives. Biochem. Biophys. Res. Commun. 22, 17–21 (1966)
Previero, A., G. Prota, and M. A. Coletti-Previero: C-Acylation of the Tryptophan lndole Ring and its Usefulness in Protein Chemistry. Biochim. Biophys. Acta 285, 269–278 (1972)
Previero, A., E. Scoffone, C. A. Benassi, and P. Pajetta: Modification of Tryptophan Residues in Peptides. Gazz. Chim. Ital. 93, 849–858 (1963)
Ponnuswamy, P. K., and V. Sasisekharan: Conformation of Amino Acids. V. Conformation of Amino Acids with δ-Atoms. Intern. J. Protein Res. 3, 9–18 (1971)
Paulos, T. L., and P. A. Price: Identification of a Tryptophan Residue Essential to the Catalytic Activity of Bovine Pancreatic Deoxyribonuclease. J. Biol. Chem. 246, 4041–4045 (1971)
Ramachandran, L. K., and B. Witkkop: N-Bromosuccinimide Cleavage of Peptides, in: Methods in Enzymology (C. H. W. Hirs, Ed.) 11, 283–299. London-New York: Academic Press. 1967
Ramachandran, J., and V. Lee: Preparation and Properties of the o-Nitrophenyl Sulfenyl Derivative of Acth: An Inhibitor of the Lipolytic Action of the Hormone. Biochem. Biophys. Res. Commun. 38, 507–512 (1970)
Ramamurthy, T. V., and L. Pichat: Preparation of High Specific Activity Dltryptophan-2,3-T and Its Resolution to L-Tryptophan-2,3-T. J. Label. Compounds 9, 325–330 (1973)
Ray, W. J., JR.: Photochemical Oxidation, in: Methods in Enzymology (C. H. W. Hirs, Ed.) 11, 490–497. London-New York: Academic Press. 1967
Reiss, A., and A. Lukton: Reactivation of Lysozyme from Inactive Hnb-Lysozyme. Biorganic Chem. 4, 1–21 (1975)
Richards, R. E., and N. A. Thomas: A Nitrogen-14 Nuclear Magnetic Resonance Study of Amino Acids, Peptides and other Biologically Interesting Molecules. I. Chem. Soc., Perkin II, 368–374 (1974)
Ridd, J. H.: Heteroaromatic Reactivity. Phys. Methods Heterocyclic Chem. 1, 109–160 (1963)
Riggle, W. L., J. A. Lang, and C. L. Borders, JR.: Reaction of Turkey Egg-white Lysozyme with Tnm. Modification of Tyrosin and Tryptophan. Can. J. Biochem. 51, 1433–1439 (1973)
Riniker, B., M. Brugger, B. Kamber, P. Sieber, and W. Rittel: Thyrocalcitonin. IV. Die Totalsynthese des α-Thyrocalcitonins. Helv. Chim. Acta 52, 1058–1073 (1969)
Rivaille, R., A. Robinson, M. Kamen, and G. Milhand: Synthese en Phase Solide de l’Hormone de Liberation de 1’Hormone Luteotrophique (LM-RH). Helv. Chim. Acta 54, 2772–2775 (1971)
Rrvetrr, D. E., and J. F. K. Wilshire: The Periodate Oxidation of Tryptophan and Some Related Compounds. Aust. J. Chem. 24, 2717–2722 (1971)
Rivett, D. E.: personal communication.
Robbins, F. M., and L. G. Holmes: Binding of N-Methylnicotinamide Chloride by Tryptophan Residues of α-Lactalbumin. J. Biol. Chem. 247, 3062–3065 (1972)
Robinson, G. W.: Reaction of a Specific Tryptophan Residue in Streptococcal Proteinase with 2-Hydroxy-5-nitrobenzyl Bromide. J. Biol. Chem. 245, 4832–4841 (1970)
Rosen, C. G., T. Gejuall, and L. O. Andersson: Reaction of Diethyl Pyrocarbonate with Indole Derivatives with Special Reference to the Reaction with Tryptophan Residues in a Protein. Biochim. Biophys. Acta. 221, 207–213 (1970)
Ruban, E. L., N. S. Mamulina, and N. I. Yukhanova: Transformation of Dtryptophan into L-Tryptophan by Flavobacterium Butyri 331. Izv. Akad. Nauk Sssr, Ser. Biol. 150–153 (1972)
Sakamura, S., and Y. Obata: A New Chemical Method for the Preparation of Kynurenine by Oxidation with Peracetic Acid. Nippon Nogei-Kagaku Kaishi (Chem. Abstr. 52, 20296a, 1955) 29, 817–819 (1955)
Sakiyama, F., and N. Masuda: Chemical Cleavage of the Peptide Bond at the Tryptophan Residue. Improved Method. Chem. Lett. 9, 949–952 (1973)
Samy, T. S. A., M. Atrey, H. Maeda, and J. Meienhofer: Selective Tryptophan Oxidation in the Antitumor Protein Neocarzinostatin and Effects on Conformational and Biological Activity. Biochemistry 13, 1007–1014 (1974)
Santarius, K., und H. D. Belitz: Eine einfache Methode zur TryptophanBestimmung in Proteinen. Z. Lebensmittel-Unters. und Forsch. 150, 280–282 (1973)
Sarges, R., and B. Witkop: Gramicidin A. VI. The Synthesis of Valine- and Isoleucine-gramicidin A. J. Amer. Chem. Soc. 87, 2020–2027 (1965).
Sasisekharan, V., and P. K. Ponnyswamy: Studies on the Conformation of Amino Acids. X. Conformations of Norvalyl, Leucyl and Aromatic Side Group in a Dipeptide Unit. Biopolymers. 10, 583–592 (1971)
Savige, W. E.: Isolation and Identification of Some Photo-Oxidation. Products of Tryptophan. Aust. J. Chem. 24, 1285–1293 (1971)
Savige, W. E.: Paper presented at the 5th Int. Wool Text. Res. Conference, Aachen (1975), Schriftenreihe, in press.
Savige, W. E.: New Oxidation Products of Tryptophan. Aust. J. Chem. 28, 2275–2283 (1975)
Schechter, Y., Y. Burstein, and A. Patchornik: Sulfenylation of Tryptophan-62 in Hen Egg White Lysozyme. Biochemistry 11, 653–660 (1972)
Schellenberg, K. A., and G. W. Mc Lean: Titration of Malate Dehydrogenase with 2-Hydroxy-5-nitrobenzyl Bromide. Biochim. Biophys. Acta 191, 727–728 (1969)
Schellenberg, K. A.: Evidence for the Participation of Tryptophan as Intermediate in Transfer of Hydrogen between Diphosphopyridine Nucleotide and Substrate in Yeast Alcohol Dehydrogenase. J. Biol. Chem. 240, 1165–1169 (1965)
Schellenberg, K. A.: Participation of Tryptophan Residues in Dehydrogenase Action. II. Position of Tritium-labelled Hydrogen in Yeast Alcohol Dehydrogenase after various Means of Inactivation and Hydrolysis. J. Biol. Chem. 241, 2446–2452 (1966)
Schellenberg, K. A.: Tryptophan as Intermediate in Dehydrogenase Action. III. Evidence for Complete Cycle of Hydrogen Transfer between Substrate and Tryptophanyl Residues in Rabbit Muscle Lactate Dehydrogenase. J. Biol. Chem. 242, 1815–1820 (1967)
Schlessinger, J., A. Grafui, and I. Z. Steinberg: Optical Rotatory Power in the Ground State and Electronically Excited State of Diketopiperazines Containing Aromatic Side Chains. J. Amer. Chem. Soc. 96, 7396–7400 (1974).
Schlessinger, J., R. S. Roche, and I. Z. Steinberg: A Study of Subtilisin Type Novo and Carlsberg by Circular Polarization of Fluorescence. Biochemistry 14, 255–262 (1975)
Schmir, G., L. Cohen, and B. Witkop: The oxidative Cleavage of Tyrosyl-Peptide Bonds. I. Cleavage of Dipeptides and Some Properties of the Resulting SpirodienoneLactones. J. Amer. Chem. Soc. 81, 2228–2233 (1959)
Schroder, E., and K. LÜBke: Synthese von Peptiden und Peptidwirkstoffen, in: Progress in the Chemistry of Organic Natural Compounds (L. Zechmeister, Ed.) 26, 48–1 19. Wien-New York: Springer. 1968
Schwyzer, R., and P. Sieber: Total Synthesis of Adrenocorticotropic Hormone. Nature 199, 172–174.
Schwyzer, R., and H. Kappeler: Synthesis of a Tetracosapeptide with high corticotropic Activity: βi–24Corticotropin. Helv. Chim. Acta 46, 1550–1572 (1963)
Schwyzer, R., B. Iselin, H. Kappeler, B. Riniker, W. Rittel, and H. Zuber: Synthesis of β-melanotropin (β-Msh) with Amino Acid Sequence of the Bovine Hormone. Helv. Chim. Acta46, 1975–1996 (1963).
Scoffone, E., and A. Fontana: Identification of Specific Amino Acid Residues. Protein Sequence Determination. Methods and Techniques (S. B. Needleman, Ed.), p. 185–210. New York: Springer. 1970
Scoffone, E., A. Fontana, and R. Rocchi: Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins. I. Modification of Tryptophan Residue. Biochemistry 7, 971–979 (1968)
Seto, A., S. Sato, and N. Tamiya: Properties and Modification of Tryptophan in a Sea Snake Toxin Erabutoxin a. Biochim. Biophys. Acta 214, 483–489 (1970)
Shaw, J. L. D., and W. D. Mcfarlane: The Determination of Tryptophan by Modified Glyoxylic Acid Method Employing Photoelectric Colorimetry. Can. J. Res. 16 B, 361–368 (1938)
Shechter, Y., A. Patchornik, and Y. Burstein: Selective Sulfenylation of Tryptophan Residues in α-Lactalbumin of Bovine Milk. J. Biol. Chem. 249, 413–419 (1974)
Sheinblatt, M.: Determination of Amino Acid Sequence in Di- and Tripeptides by Nuclear Magnetic Resonance Techniques. J. Amer. Chem. Soc. 88, 2845–2848 (1966)
Shelton, K. R., and K. S. Rogers: Tryptophanyl Fluorescence of Sodium Dodecyl Sulfate Treated and 2-Mercaptoethanol Reduced Proteins: A simple Assay for Tryptophan. Anal. Biochem. 44, 134–142 (1971)
Shinitzky, M., Y. Dudai, and I. Siluran: Spectral Evidence for the Presence of Tryptophan in the Binding Site of Acetylcholinesterase. Febs Lett. 30, 125–128 (1973)
Skye, G. F., R. Potts, and H. G. Floss: Stereochemistry of the Tryptophan Synthetase Reaction. J. Amer. Chem. Soc. 96, 1593–1595 (1974)
Sievertsson, H., J. K. Chang, C. Bogentoft, B. L. Currie, K. Folkers, and C. Y. Bowers: Synthesis of the Luteinizing Relasing Hormone of the Hypothalamus and its Hormonal Activity. Biochem. Biophys. Res. Commun. 44, 1566–1571 (1971).
Slifkin, M. A.: in: “Charge Transfer Interactions of Biomolecules” (M. A. Slifkin, Ed.), Chapter 3, Amino Acids and Proteins, p. 52–75. London-New York: Academic Press. 1971
Slifkin, M. A.: in: “Charge Transfer Interactions of Biomolecules” (M. A. Slifkin, Ed.), Chapter 5, Indoles and Imidazoles, p. 97–117. London-New York: Academic Press. 1971
Slump, P., and H. A. W. Schrender: Determination of Tryptophan in Foods. Anal. Biochem.0, 182–186 (1968)
Sokolovsky, M., D. Harell, and J. F. Riordan: Reactions of Tetranitromethane with Sulfhydryl Groups in Proteins. Biochemistry 8, 4740–4745 (1969)
Sokolovsky, M., J. F. Riordan, and B. L. Vallee: Tetranitromethane. Reagent for the Nitration of Tyrosyl Residues in Proteins. Biochemistry 5, 3582–3589 (1966)
Sokolovsky, M., M. Fuchs, and J. F. Riordan: Reaction of Tetranitromethane with Tryptophan and Related Compounds. Febs Lett. 7, 167–170 (1970)
Spackman, D. H., W. H. Stein, and S. Moore: Automatic Recording Apparatus for Use in the Chromatography of Amino Acids. Anal. Chem. 30, 1190–1205 (1958).
Spande, T. F., A. Fontana, and B. Witkkop: An Unusual Reaction of Skatole with Tetranitromethane. J. Amer. Chem. Soc. 91, 6199–6200 (1969)
Spande, T. F., and A. Fontana: unpublished results, reported in ref. 123 and 375.
Spande, T. F., and B. Witkop: Reactivity toward N-Bromosuccinimide as a Criterion for Buried and Exposed Tryptophan Residues in Proteins, in: Methods in Enzymology (C. H. W. HIrs, Ed.). 11, p. 522–528. London-New York: Academic Press. 1967
Spande, T. F., and B. Witkop: Determination of the Tryptophan Content of Proteins by N-Bromosuccinimidc, in: Methods in Enzymology (C. H. W. Hirs, Ed.). 11, p. 498–506. London-New York: Academic Press. 1967
Spande, T. F., and B. Witkop: Tryptophan Involvement in Binding Sites of Proteins and in Enzyme-Inhibitor Complexes as Determined by Oxidation with N-Bromosuccinimide, in: Methods in Enzymology (C. H. W. Hirs, Ed.). 11, p. 506–522. London-New York: Academic Press. 1967
Spande, T. F., B. Witkop, Y. Degani, and A. Patchornik: Selective Cleavage and Modification of Peptides and Proteins. II. Advan. Protein Chem. 24, 97–260 (1970)
Spande, T. F., and G. G. Glenner: The Reaction of Indoles with a Diazonium Salt (Fast Red B). J. Amer. Chem. Soc. 95, 3400–3401 (1973)
Spande, T. F., N. M. Green, and B. Witkop: The Reactivity toward N-bromosuccinimide of Tryptophan in Enzymes, Zymogens, and Inhibited Enzymes. Biochemistry 5, 1926–1933 (1966)
Spande, T. F., M. Wilchek, and B. Witkop: The Reaction of Derivatives of Tryptophan, Tryptamine, and Other Indoles with 2-Hydroxy-5-nitrobenzyl Bromide (Koshland’s Reagent). J. Amer. Chem. Soc. 90, 3256–3258 (1968)
Spies, J. R., and D. C. Chambers: Determination of Tryptophan with p-Dimethylaminobenzaldehyde Using Photochemical Development of Color. Anal. Chem. 22, 1209–1210 (1950)
Spies, J. R., and D. C. Chambers: Chemical Determination of Tryptophan in Proteins. Anal. Chem. 21, 1249–1266 (1949)
Steinberg, I. Z., J. Schlessinger, and A. Gafin: Application of Circular Polarization of Luminescence to the Study of Peptides, Polypeptides and Proteins, in: Peptides, Polypeptides, and Proteins (E. R. Blout, F. A. Bovey, M. Goodman, and N. Lotan, Eds.), p. 351–369. New York-London: J. Wiley. 1974
Steitz, T. A., R. Henderson, and D. M. Blow: Structure of Crystalline αChymotrypsin. III. Crystallographic Studies of Substrates and Inhibitors Bound to the Active Site of α-Chymotrypsin. J. Mol. Biol. 46, 337–348 (1969)
Stellwagen, E., and S. Van Rooyan: The Structural Environement of the Tryptophanyl Residue of Horse Heart Ferricytochrome C. J. Biol. Chem. 242, 4801–4805 (1967)
Stevens, L., R. Townend, S. N. Timasheff, G. D. Fasman, and J. Potter: The Circular Dichroism of Polypeptide Films. Biochemistry 7, 3717–3720 (1968)
Stewart, M., and C. H. Nicholls: Kinetic Study of the Acid Autoxidation of Tryptophan. Aust. J. Chem. 25, 2139–2144 (1972)
Stewart, M., and C. H. Nicholls: A Kinetic Study of the Alkali Degradation of Tryptophan. Aust. J. Chem. 25, 1595–1599 (1972)
Stewart, M., and C. H. Nicholls: A kinetic Study of the Autoxidation of Tryptophan at 100° C in the pH Range 2–7. Aust. J. Chem. 27, 205–208 (1974)
Stohrer, G., G. Salemnick, and G. B. Brown: A Chemical Adduct of Tryptophan and the Oncogen 3-Acetoxyxanthine. Biochemistry 12, 5084–5086 (1973)
Strickland, E. H., M. Wilchek, J. Horwitz, and C. Billups: Low Temperature Circular Dichroism of Tyrosyl and Tryptophanyl Diketopiperazines. J. Biol. Chem. 245, 4168–4177 (1970)
Strickland, E. H., C. Billups, and E. Kay: Effects of Hydrogen Bonding and Solvents upon the Tryptophanyl 1La Absorption Band-Studies Using 2,3-Dimethylindole. Biochemistry 11, 3657–3662 (1972)
Strickland, E. H., and C. Billups: Oscillatory Strengths of the 1La and 1Lb Absorption Bands of Tryptophan and Several Other Indoles. Biopolymers 12, 1989–1995 (1973)
Strickland, E. H., J. Horwitz, and C. Billups: Fine Structure in the NearUltraviolet Circular Dichroism and Absorption Spectra of Tryptophan Derivatives and Chymotrypsinogen A at 77° K. Biochemistry 8, 3205–3213 (1969)
Sumpter, W. C., and M. Miller: The Chemistry of Heterocyclic Compounds (A. Weissberger, Ed.), lnterscience 8. New York: J. Wiley. 1954
Sundberg, R. J.: The Chemistry of Indoles. London-New York: Academic Press. 1970
Sundberg, R. J.: The Chemistry of Indoles, p. 17–18. London-New York: Academic Press. 1970
Sundberg, R. J.: The Chemistry of Indoles, p. 19–31. London-New York: Academic Press. 1970
Sundberg, R. J.: The Chemistry of Indoles, p. 39–56. London-New York: Academic Press. 1970
Sundberg, R. J.: The Chemistry of Indoles, p. 78–83. London-New York: Academic Press. 1970
Sundberg, R. J.: The Chemistry of Indoles, p. 83–85. London-New York: Academic Press. 1970
Sundberg, R. J.: Thc Chemistry of Indoles, p. 142–163. London-New York: Academic Press. 1970
Sundberg, R. J.: The Chemistry of Indoles, p. 230–235. London-New York: Academic Press. 1970
Sundberg, R. J.: The Chemistry of Indoles, p. 282–312. London-New York: Academic Press. 1970
Suzki, S., Y. Hachimori, and U. Yaoeda: Spectrophotometric Determination of Glycine with 2,4,6-trichloro-5-triazine. Anal. Chem. 42, 101–103 (1970)
Takahashi, K.: Structure and Function of Ribonuclease T1. Viii. Reaction of 2-hydroxy-5-nitrobenzyl Bromide with the Single Tryptophan Residue in Ribonuclease T1. J. Biochem. (Tokyo) 67, 541–547 (1970)
Takigawa, T., T. AshiDA, Y. Sasada, and M. Kakudo: The Chrystal Structures of L-Tryptophan Hydrochloride and Hydrobromide. Bull. Chem. Soc. Japan 39, 2369–2378 (1966)
Terui, G.: Tryptophan, in: The Microbial Production of Amino Acids (Yamada, K., S. Kinoshita, T. Tsunoda, and K. Aidda, Eds.), p. 515–531. New York: J. Wiley. 1974
Teuwissen, B., P. L. Masson, P. Osinski, and J. F. Hermans: Metal-combining Properties of Human Lactoferritin. Effect of Nitration of Lactoferritin with Tetranitromethane. Eur. J. Biochem. 35, 366–371 (1973)
Toniolo, C.: Relationship among Primary Structures, Conformations, and Biological Activities of Polypeptide Antibiotics. II Farmaco, Ed. Sci. 26, 741–769 (1971)
Turner, D. H., I. TlNoco, JR., and M. Maestre: Fluorescence Detected Circular Dichroism. J. Amer. Chem. Soc. 96, 4340 4342 (1974)
Udenfriend, S.: Proteins and Peptides, in: Fluorescence Assay in Biology and Medicine, 2, Chapter 6, p. 248–283. London-New York: Academic Press. 1969
Udenfriend, S.: Amino Acids, Amines, and their Metabolites, in: Fluorescence Assay in Biology and Medicine. 2, Chapter 5, p. 195–247. London-New York: Academic Press. 1969
Ulmer, D. D.: Tyrosine and Tryptophan in Cytochrome C. Biochemistry 5, 1886–1892 (1966)
Vallee, B. L., and J. F. Riordan: Chemical Approachs to the Properties of Active Sites of Enzymes. Ann. Rev. Biochem. 38, 733–794 (1969)
Veatch, W. R., E. T. Fossel, and E. R. Blout: The Conformation of Gramicidin A. Biochemistry 13, 5249–5256 (1974)
Veronese, F. M., E. BoCCÙ, C. A. Benassi, and E. Scoffone: Preferential Hydrolysis of Kynurenine Peptides. Z. Naturforsch. 24, 294–300 (1969)
Veronese, F. M., E. Boccu, and A. Fontana: Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins. V. The Use of 2-Nitro-4-Carboxyphenylsulfenyl Chloride. Ann. Chim. (Rome) 58, 1309–1319 (1968)
Veronese, F. M., E. Boccu, and A. Fontana: Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins. VI. 2,4-Dinitrophenyl-1,5-disulfenyl Chloride, a Cross-linking Reagent for Tryptophan Residues. Int. J. Protein Res. 2, 67–74 (1970)
Veronese, F. M., E. Boccu, and A. Fontana: Modification of Tryptophan-108 of Lysozyme with 2-Nitro-4-carboxyphenylsulfenyl Chloride. Febs Lett. 21, 277–280 (1972)
Veronese, F. M., A. Fontana, E. BoccÙ, and C. A. Benassi: Synthesis of Kynurenine Peptides. Gazz. Chim. Ital. 97, 321–331 (1967)
Veronese, F. M., A. Fontana, E. BoccÙ, and C. A. Benassi: Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins. IV. On the Conversion of 2-Thioaryl-Tryptophan to 2-Hydroxy-tryptophan. Z. Naturforsch. 23b, 1219–1325 (1968)
Voelkl, A., and G. Quadbeck: New Color Reaction to Identify Indoles. Arztl. Lab. 19, 45–50 (1973)
Voetter, W., G. Jung, E. Breitmaier, and E. Bayer: Carbon-13 Nmr Chemical Shifts of Amino Acids and Peptides. Z. Naturforsch. 26b, 213–222 (1971)
Walrant, P., and R. Santus: N-Formylkynurenine, a Tryptophan Photooxidation Product, as a Photodinamic Sensitizer. Photochem. Photobiol. 19, 411–417 (1974)
Walrant, P., and R. Santus: Ultraviolet and N-Formyl-kynurenine Sensitized Photoinactivation of Bovine Carbonic Anhydrase: an Internal Photodinamic Effect. Photochem. Photobiol. 20, 455–460 (1974)
Weil, L., W. G. Gordon, and A. R. Buchert: Photooxidation of Amino Acids in the Presence of Methylene Blue. Arch. Biochem. Biophys. 33, 90–109 (1951)
Westhead, E. K.: Dye-Sensitized Photooxidation, in: Methods in Enzymology (C. H. W. Hirs and S. N. Timasheff, Eds.), 25, p. 401–409. London-New York: Academic Press. 1972
Wieland, T. H.: Aspects on Syntheses of Biologically Active Peptides, in: Peptides, Proc. 12th Eur. Symp. Reinhardsbrunn Castle 1972 (H. Hanson and H.-D. Jakubke, Eds.), p. 38–49. Amsterdam: North Holland Publ. Co. 1973
Wieland, TH., C. Jochum, and H. Faulstich: Optimization of the Synthesis of 2-Indole Thioethers from Derivatives of Tryptophan and Cysteine. Liebigs Ann. Chem. 727, 138–142 (1969)
Wieland, TH., M. P. Jordan DE Urries, H. Indest, H. Faulstich, A. Gieren, M. Sturm, and W. Hoppe: Components of the Green Deathcap Toadstoal, Amanita phalloides, Xlv. The Absolute Configurations of the Toxic and Nontoxic Phalloidin Sulfoxide and of the Amatoxins. Liebigs Ann. Chem. 1974, 1570–1579.
Wieland, TH., and B. Sarges: Synthesis of Tryptathionine Peptides. Liebigs Ann. Chem. 658, 181–193 (1962)
Wieland, TH., O. Weiberg, W. Dilger, and E. Fischer: Synthesis of 2-hydroxytryptophan and 2-mercaptotryptophan. Liebigs Ann. Chem. 592, 69–80 (1955)
Wilchek, M., and T. Miron: The Isolation of Tryptophan-containing Peptides by Affinity Chromatography. Biochim. Biophys. Acta 278, 1–7 (1972)
Wilchek, M., and T. Miron: Conversion of Tryptophan to 2-Thioltryptophan in Peptides and Proteins. Biochem. Biophys. Res. Commun. 47, 1015–1020 (1972)
Wilchek, M., T. Spande, G. Milne, and B. Witkoe: The Nonenzymatic Conversion of Tyrosine into Mono- and Dihydroxyindoles. Biochemistry 7, 1777–1786 (1968)
Wilchek, M., and B. Witkop: Protection of Tryptophan During Cleavage of Tyrosine Peptide Bonds by N-Bromosuccinimide. Biochem. Biophys. Res. Commun. 26,296–300.
Williams, D. C., and J. R. Whitaker: Kinetics of Papain-catalyzed Hydrolyses of Neutral Substrates. Biochemistry 6, 3711–3717 (1967).
Witkop, B.: Directed Oxidations in the Indole Series. II. A New Method of Reaction of Perbenzoic Acid. Liebigs Ann. Chem. 558, 91–98 (1947)
Witkop, B.: Selective Modification and Cleavage of Proteins. Advan. Protein Chem. 16, 221–321 (1961)
Witkop, B.: Miscellaneous Nonenzymatic Cleavages of the Peptide Bond, in: Methods in Enzymology (C. H. W. Hirs, Ed.), 11, 308–315. London-New York: Academic Press. 1967
Witkop, B.: Chemical Cleavage of Proteins. Selective Fragmentations Reveal Structure. Science 162, 318–322 (1968)
Witkop, B., and G. Graser: Decomposition of Indole Derivatives by Means of Ozone. Liebigs Ann. Chem. 556, 103–114 (1944).
Witkop, B., and J. B. Patrick: Mechanism of Oxidation. I. New Type of Peroxide Rearrangement Catalyzed by Acid. J. Amer. Chem. Soc. 73, 2196–2200 (1951)
Witkop, B., and L. K. Ramachandran: Progress in Nonenzymic Selective Modification and Cleavage of Proteins. Metabolism 13, 1016–1025 (1964).
Witzemann, V., R. Koberstein, H. Sund, L Rasched, H. Jornvall, and K. Noack: Studies on Glutamate Dehydrogenase: Chemical Modification and Quantitative Determination of Tryptophan Residues. Eur. J. Biochem. 43, 319–325 (1974)
Wolf, H.: Studies on Tryptophan Metabolism in Man, Virum Costars Bogstrykkeri (1974)
WÜÜNsch, E.: Die Totalsynthese des Pankreas-Hormons Glucagon. Z. Naturforsch. 226, 1269–1276 (1967)
WÜÜNsch, E., A. Fontana und F. Drees: Zur Entacyclierung von Nα-(2-Nitrophenylsulfenyl)-Peptiden bei Anwesenheit von Tryptophan in der Peptidsequenz. Z. Naturforsch. 22b, 607–609 (1967)
Yamada, S., M. Yamamoto, and I. Chibata: Optical Resolution of DL-Amino Acids by Preferential Crystallization Procedure. J. Org. Chem. 38, 4408–4412 (1973)
Yamada, H., H. Yoshida, H. Nakazawa, and H. Kumagai: Microbiological Synthesis of Tryptophan and its Related Amino Acids. 1st Inter. Symp. on Tryptophan Metabolism, Acta Vitam. et Enzymologica (Milan) (1975), in press.
Yamamoto, Y., and J. Tanaka: Polarized Absorption Spectra of Crystals of Indole and its Related Compounds. Bull. Chem. Soc. Japan. 45, 1362–1366 (1972)
Yamashiro, D., and C. H. LI: Protection of Tryptophan with the Formyl Group in Peptide Synthesis. J. Org. Chem. 38, 2594–2597 (1973)
Yanaihara, N., T. Hashimoto, C. Yanaihara, K. Tsuji, Y. Kenmochi, F. Ashizawa, T. Kaneko, H. Oka, S. Saito, A. Arimura, and A. V. Schally: Syntheses and Biological Evaluation of Analogs of Luteinizing Hormone-Relasing Hormone (Lhrh) modified in Position 2, 3, 4 or 5. Biochem. Biophys. Res. Commun. 52, 64–73 (1973)
Yanaihara, N., C. Yanaihara, G. Dupuis, J. Beacham, R. Camble, and K. Hofmann: Studies on Polypeptides. Xlii. Synthesis and Characterization of Seven Fragments Spanning the Entire Sequence of Ribonuclease T1. J. Amer. Chem. Soc. 91, 2184–2185 (1969)
Yonemitsu, O., K. Miyashita, Y. Ban, and Y. Kanaoka: Polyphosphate Ester as a Synthetic Agent. XI. A Novel Synthesis of Ethylindolenincs by Ethylation of 2,3Disubstituted Indoles with Polyphosphate Ester. Tetrahedron 25, 95–100 (1969)
Yutaka, 1H., H. Hiroo, K. Kenzo, and S. Kazoo: States of Amino Acid Residues in Proteins. V. Different Reactivities with H2O2 of Tryptophan Residues in Lysozyme, Protcinases, and Zymogens. Biochim. Biophys. Acta 93, 346–360 (1964)
Zahnley, J. C., and J. G. Davis: Effect of High Tyrosine Content on the Determination of Tryptophan in Protein by the Acidic Ninhydrin Method. Application to Chicken Ovoinhibitor. Biochem. J. 135, 59–61 (1973)
Zaporozhets, E. V., I. A. Avrutskaya, K. K. Babievskii, V. M. Belikov, and M. Fioshin: Electrochemical Reduction of the Methyl Ester of α-nitro-3(3-indolyl)acrylic acid. Elektrokhimiya 8, 1243–1245 (1972)
Zaporozhets, E. V., I. A. Avrutskaya, M. YA. Fioshin, K. K. Babievskii, and V. M. Belikov: Effect of Electrode Material on the Electroreduction of Indolylnitroacrylate. Elektrokhimiya 9, 72–76 (1973)
Enfield, D. L., L. H. Ericsson, K. A. Walsh, H. Neurath, and K. Titani: Bovine Factor X1 (Stuart Factor). Primary Structure of the Light Chain. Proc. Nat. Acad. Sci. Usa 72, 1619 (1975)
Jesty, J., A. K. Spencer, Y. Nakashima, Y. Nemerson, and W. Konigsberg: The Activation of Coagulation Factor X. Identity of Cleavage Sites in the Alternative Activation Pathways and Characterization of the Cooh- Terminal Peptide. J. Biol. Chem. 250, 4497–4504 (1975)
Karkhanis, Y. D., D. J. Carlo, S. W. Brostoff, and E. H. Eylar: Allergic Encephalomyelitis. Isolation of an Encephalitogenic Peptide Activc in the Monkey. J. Biol. Chem. 250, 6141–6150 (1975)
Levy, P. L., M. K. Pangburn, Y. Burstein, L. H. Ericsson, H. Neurath, and K. A. Walsh: Evidence of Homologous Relationship between Thermolysin and neutral Protease A of Bacillus subtilis. Proc. Nat. Acad. Sci. Usa 72, 4341–4345 (1975)
Rynbrandt, R. M.: The Reaction of Sulfoxides with Hydrogen Chloride. Tetrahedron Letters 381, 3553–3555 (1971)
Savige, W. E., and A. Fontana: paper in preparation (1975)
Scorrano, G.: Equilibria and Reactions of Organic Sulfoxides in Moderately Concentrated Acids. Accounts Chem. Res. 6, 132–138 (1973)
Spande, T. F., and G. G. Glenner: The Reaction of a Tryptophan Derivative with the Diazonium Salt, “Fast Red B”, unpublished work (1975)
Titani, K., L. H. Ericsson, K. A. Walsh, and H. Neurath: Amino Acid Sequence of Bovine Carboxypeptidase B. Proc. Natl. Acad. Sci. Usa 72, 1666–1670 (1975)
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1976 Springer-Verlag Wien
About this chapter
Cite this chapter
Fontana, A., Toniolo, C. (1976). The Chemistry of Tryptophan in Peptides and Proteins. In: Herz, W., Grisebach, H., Kirby, G.W. (eds) Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products. Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products, vol 33. Springer, Vienna. https://doi.org/10.1007/978-3-7091-3262-3_4
Download citation
DOI: https://doi.org/10.1007/978-3-7091-3262-3_4
Publisher Name: Springer, Vienna
Print ISBN: 978-3-7091-3264-7
Online ISBN: 978-3-7091-3262-3
eBook Packages: Springer Book Archive