Abstract
Now that mass spectrometric techniques can be applied to a much wider range of molecules, the problem of searching the literature in order to find out whether or not the mass spectrum of a particular analyte has been reported has increased significantly. For example, many reports of mass spectral data now may be found in journals with which the mass spectrometrist is almost certainly unfamiliar. In this connection, it might be thought that the ready availability of a number of computerized bibliographic databases would mean that this problem can easily be solved by using the most appropriate database. The purpose of the present chapter is to show, by means of a detailed consideration of the reporting of a key biochemical analyte, human hemoglobin, that this is not the case, since a number of key references are overlooked. The reasons for this finding, which confirm previous Salford studies on the efficiency of literature databases for small molecules (1,2), are first that none of the databases cover 100% of the scientific literature and, second, no system is 100% efficient in its abstracting of experimental measurements published in scientific papers. The reason for the choice of human hemoglobin to illustrate this data searching problem is that one of us had conducted joint research with the late Professor M. Barber on the measurement of the mass spectra of intact globins using fast-atom bombardment-mass spectrometry techniques (3), and this research interest is still maintained by the first author (4).
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References
Brooks, C. T. (1980) Computer Production and Analysis of a Fully Indexed Bibliographic Database on Oestrogen Methodologies. PhD. Thesis, University of Salford, UK.
Blunden-Ellis, J. C. P. (1984) Bibliographic Analysis of the Literature of the HPLC Methods for Separating PTH-Amino Acids. MSc Thesis, University of Salford, UK.
Barber, M., Bell, D., Morris, M., Tetler, L. W., Woods, D., Gordon, D. B., Garner, G. V., Airey, C. J., Croft, L. R., and Oliver, R. W. A. (1988) Mass Spectral Analysis of Aberrant Haemoglobins. 11th International MS conference, Bordeaux, France, September.
Green, B. N., Quaife, R., Hassounah, F. H., and Oliver R. W. A. (1996) On the combined use of mass spectrometric and genetic analytical techniques to Identify hemoglobm variants. Hemoglobin, in press.
Appendix
Bookchin, R. M. and Gallop, P. M. (1968) Structure of hemoglobin A,,-nature of the N-terminal P-chain blocking group. Biochem. Biophys. Res. Commun. 32, 86–93. xxx
Morris, H. R. and Willlams, D. H. (1972) The identification of a mutant peptide of an abnormal haemoglobin by mass spectrometry. J. Chem. Soc. Chem. Commun. 114–116. XXX.
Wada, Y., Fugita, T., Hayashi, A., Matsuo, T., Katakuse, I, and Matsuda, H. (1980) I. Structural analysis of human hemoglobin variants by field desorption mass spectrometry. Iyo Masu Kenkyukai Koenshu 5, 135–140 (Japanese) XCX.
Matsuo, T., Matsuda, H., Katakuse, I., Wada, Y., Fujita, T., and Hayashi., A. (1981) Field desorption mass spectra of tryptic peptides of human hemoglobin chains. Biomed. Mass Spectrom. 8, 25–30. BCX.
Wada, Y., Hayashi, A., Fujita, T., Matsuo, T., Katakuse, I., and Matsuda, M. (1981) Structural analysis of human hemoglobin variants with field desorption mass spectrometry. Biochim. Biophys. Acta. 667, 233–241. BCM.
Aschauer, H., Schafer, W., Sanguansermsri, T., and Braunitzer, G. (1981) Human embryonic haemoglobins. Ac-Ser-Leu-Thr-is the N-terminal sequence of the zeta-chains. Hoppe Seyler’s Z Physiol. Chem. 362, 1657–1659. XCM.
Matsuo, T., Katakuse, I., Matsuda, H., Wada, Y., Fujita, T., and Hayashi, A. (1981) II. Field desorption mass spectra of peptide mixture of human globin digested by thermolysin and staphyloccal protease. Iyo Masu Kenkyukai Koenshu 6, 107–110. (Japanese) XCX.
Wada, Y., Hayashi, A., Matsuo, T., Sakurat, T., Matsuda, H., and Higuchi, T. (1982) Structural analysis of human hemoglobin variants by mass spectrometry III. Comparison of FD and FAB mass spectra and identification of homozygosity for T-gamma globin by mass spectrometry. Iyo Masu Kenkyukai Koenshu 7, 123–126. (Japanese) XCX.
Wada, Y., Hayashi, A., Matsuo, T., Sakurai, T., Matsuda, H., and Katakuse, I. (1983) Structural analysis of human hemoglobin variants by mass spectrometry IV. Characterisation of two new hemoglobin variants by FDMS and molecular SIMS. Iyo Masu Kenkyukai Koenshu 8, 209–212. (Japanese) XCX.
Wada, Y., Hayashi, A., Fujita, T., Matsuo, T., Katakuse, I., and Matsuda, H. (1983) Structural analysis of human hemoglobin variants by mass spectrometry. Int. J. Mass Spectrom. Ion. Phys. 48, 209–212. BCX.
Wada, Y., Hayashi, A., Masanori, F., Katakuse, I., Ichihara, T., Nakabushi, H., Matsuo, T., Sakurai, T., and Matsuda, H. (1983) Characterisation of a new fetal haemoglobin variant, Hb F Izumi Aγ (6) Glu → Gly, by molecular secondary ion mass spectrometry. Biochim. Brophys. Acta. 749, 244–248. XCM.
Katakuse, I., Ichihara, T., Nakabushi, H., Matsuo, T., Matsuda, H., Wada, Y., and Hayashi, A. (1984) Secondary ion mass spectra of tryptic peptides of human hemoglobin chains. Biomed. Mass Spectrom. 11, 386–391. BXM.
Puccl, P., Carestia, C., Fioretti, G., Mastrobuoni, A. M., and Pagano, L. (1985) Protein finger printing by FAB. Characterisation of normal and variant human haemoglobms. Biochem. Biophys. Res. Commun. 130, 84–90. XCM.
Wada, Y., Hayashi, A., Matsuo, T., Matsuda, H., and Katakuse, I. (1985) Structural analysis of human hemoglobin variants by mass spectrometry. V Characterisation of a foetal hemoglobin variant in the extract from dried blood on filter paper. Iyo Masu Kenkyukai Koenshu 10, 87–90 (Japanese) XCX.
Fujita, S., Ohta, Y., Saito, S., Kobayashi, Y., Naritomi, Y., Kawaguchi, K., Imamura, T., Wada, Y., and Hayashi, A. (1985) Hemoglobin A2 Honai α282(90) Glu → Val: a new delta chain variant. Hemoglobin. 9(6), 597–607. XXX.
Wada, Y., Hayashi, A., Katakuse, I., Matsuo, T., and Matsuda, H. (1985) Application of glycinamidation to the peptide mapping using secondary ion mass spectrometry. Biomed. Mass Spectrom. 12, 122–126. XXX.
Rahbar, S., Louis, J., Lee, T., and Asmerom, Y. (1985) Hemoglobin North Chicago, β(36) Pro → Ser: A new high affinity hemoglobin. Hemoglobin 9, 559–576. XXM.
Boissel, J-P., Kasper, T. J., Shah, S. C., Malone, J. I., and Bunn, H. F. (1986) Amino-terminal processing of proteins. Hemoglobin South Florida Proc. Natl. Acad. Sci. USA 82, 8448–8452. XXM.
Wada, Y., Fujita, T., Kidoguchi, K., and Hayashi, A. (1986) Foetal haemoglobin variants in 80,000 Japanese neonates: high prevalence of Hb F Yamaguchi AγT(so) Asp → Asn. Hum. Genet. 72, 196–202. XXX.
Rahbar, S., Lee, T. D., Baker, J. A., Rabinowitz, L. T., Asmerom, Y., Legesse, K., and Ranney, H. M. (1986) Reverse phase HPLC and SIMS: A strategy for identification of ten human hemoglobin variants. Hemoglobin 10, 379–400. BCM.
Blouquit, Y., Rhoda, M. D., Delanoe-Garin, J., Rosa, R., Prome, J. C., Poyart, C., Puzo, G., Bernassaus, J. M., and Rosa, J. (1986) Glycerated hemoglobin α2β2(82)N-ε-glyceryllysine. a new post-translational modification occurring in erythrocyte bisphosphoglyceromutase deficiency. J. Biol. Chem. 261, 6758–6764. XCX.
Matsuo, T., Sakurai, T., Katakuse, I., Matsuda. H., Wada, Y., and Hayashi, A. (1986) Amino acid sequencing of peptide mixtures. structural analysis of human hemoglobin variants (Digit Printing Method). Springer Proc. Phys. 9, 113–117. XCX.
Castagnola, M., Landolfi, R., Rossetti, D., DeAngelis, F., and Ceccarelli, S. (1986) Determination of abnormal hemoglobins by the combined use of reversed phase high performance liquid chromatography and fast atom bombardment mass spectrometry. Anal. Lett. 19, 1793–1807. XCX.
Wada, Y. (1986) Structural analysis of variant protein by mass spectrometry. Iyo Masu Kenkyukai Koenshu 11, 55–60. (Japanese) XXX.
Hidaka, K. and Iuchi, I. (1986) Hemoglobin J-Norfolk found in the Kobe District. Kawasaki Med. J. 12, 97–99. (Japanese) XCX.
Hayashi, A., Wada, Y., Matsuo, T., Katakuse, L., and Matsuda, H. (1987) Neonatal screening and mass spectrometric analysis of hemoglobin variants in Japan. Acta. Haematol. 78, 114–118. XXM.
Wada, Y., Ikkala, E., Imat, K., Matsuo, T., Matsuda, H., Lehtinen, M., Hayashi, A., and Lehmann, H. (1987) Structure and function of a new hemoglobin variant Hb: Meilahti α2β2(36)Pro → Thr, characterised by mass spectrometry. Acta. Haematol. 78, 109–113. XCM.
Prome, D., Prome, J. C., Blouquit, Y., Lacombe, C., Rosa, J., and Robinson, J. D. (1987) FAB mapping of proteins: detection of mutation sites in abnormal human hemoglobins. Spectros. Int. J. 5, 157–170. XCX.
Wada, Y. and Hayashi, A. (1987) Structural analysis of hemoglobin by mass spectrometry: a review. Tanpakushitsu Kakusan Koso 32, 697–703. (Japanese) XXM.
Blouquit, Y., Rhoda, M. D., Delanoe-Garin, J., Rosa, R., Prome, J. C., Poyart, C., Puzo, G., Bernassaus, J. M., and Rosa, J. (1987) Glycerated hemoglobin α2β2(82) N-ε-glyceryllysine: a new post-translational modification occuring in erythrocyte bisphosphoglyceromutase deficiency. Biomed. Biochim. Acta. 46, S202–S206. XXX.
Castognola, M., Dobasz, M., Landolfi, R., Pascali, V. L., deAngelis, F., Vettore, L., and Perona, G. (1988) Determination of neutral haemoglobin variants by immobilized pH gradient, reversed-phase high-performance liquid chromatography and fast-atom bombardment mass spectrometry—the case of Hb Torino α(43)Phe → Val. Biol. Chem. Hoppe. Seyler. 369, 241–246. XXM.
DeBiasi, R., Spiteri, D., Caldora, M., Iodice, R., Pucci, P., Malorni, A., Ferranti, P., and Marino, G. (1988) Identification by fast atom bombardment mass spectrometry of Hb Indianapolis β(112)Cys → Arg in a family from Naples, Italy. Hemoglobin 12, 323–336. XXM.
Keitt, A. S. and Jones, R. T. (1988) The variant fetal hemoglobin F Texas I is abnormally acetylated. Am. J. Hematol. 28, 47–52. XCM.
Prome, D., Prome, J. C., Pratbernou, F., Blouquit, Y., Galacteros, F., Lacombe, C., Rosa, J., and Robinson, J. D. (1988) Identification of some abnormal haemoglobins by fast atom bombardment mass spectrometry and fast atom bombardment tandem mass spectrometry. Biomed. Environ. Mass Spectrom. 16, 41–44. XCM.
Wada, Y., Hayashi, A., Matsuo, T., and Sakurai, T. (1988) Analysis of protein variants by high performance mass spectrometer. Iyo Masu Kenkyukai Koenshu 13, 187–190. (Japanese) XCX.
Rahbar, S., Rosen, R., Nozari, G., Lee, T. D., Asmeron, Y., and Wallace, R. B. (1988) Hemoglobin Pasadena. Am. J. Hematol. 27, 204–208. XCM.
Pucci, P., Ferranti, P., Marino, G., and Malorni, A. (1989) Characterisation of abnormal human haemoglobins by fast atom bombardment mass spectrometry. Biomed. Environ. Mass Spectrom. 18, 20–26. XCM.
Molchanova, T. P., Mirgorodskaya, O. A., Abaturov, L. V., Podtelezhnikov, A. V., Yu, Tokarev, N., and Grachev, S. A. (1989) Location of amino acid substitutions in human hemoglobin. Mass spectrometric rapid analysis of tryptic peptides. Mol. Biol. (USSR) 23, 225–239 (Russian) XCM.
Wada, Y., Hayashi, A., Oka, Y., Matsuo, T., Sakurai, T., Matsuda, H., and Katakuse, I. (1989) Mass spectrometric characterisation of a haemoglobin variant, haemoglobin Riyadh. Int. J. Mass Spectrom. Ion. Proc. 91, 79–84. XCX.
Liu, S., Ren, B., He, W., Wen, H., and Weng, Q. (1989) New methods for determining amino acid sequences: FAB-mass spectroscopy. Shengwu Huaxue Zazhi 5, 97–101 (Chinese) XXX.
Wada, Y., Fujita, T., Hayashi, A., Sakurai, T, and Matsuo, T. (1989) Structural analysis of protein variants by mass spectrometry. Characterisation of haemoglobin Providence using a grand-scale mass spectrometer. Biomed. Environ. Mass Spectrom. 18, 563–565. XXM.
Wada, Y., Matsuo, T., and Sakurai, T. (1989) Structure elucidation of hemoglobin variants and other proteins by digit-printing method. Mass Spectrometry Rev. 8, 379–434. XXX.
Stachowiak, K. and Dyckes, D. F. (1989) Peptide mapping using thermospray LC/MS detection. rapid identification of hemoglobin variants. Pept. Res. 2, 267–274. XXM.
Pucci, D., Marino, G., Ferranti, P., and Malorni, A. (1989) Identification by FAB-MS of hemoglobin Indianapolis in a family from Naples. Adv. Mass Spectrom. 11, 1428,1429 XXX.
Malomi, A., Pucci, P., Ferranti, P., and Marino, G. (1989) Mass spectrometric analysis of human hemoglobin variants. Chim. Oggi. 7, 57–60. XCX.
Pucci, P., Ferranti, P., Malorni, A., and Marino, G. (1989) Spettrometria di massa FAB nello studio delle emoglobinopatie. G. Ital. Chim. Clin. 14, 115–121. (Italian) XCX.
Foldi, J., Horanyi, M., Szelenyi, J. G., Hollan, S. R., Aseeva, E. A., Lutsenko, I. N., Spivak, V. A., Toth, O., and Rozynov, B. V. (1989) Hemoglobin Siriraj found in the Hungarian population. Hemoglobin 13, 177–180. XXX.
Ferranti, P. (1989) Caratterizzazione di varianti genetiche dell’emoglobina umana mediante spettrometria di massa FAB. Chim. Ind. 71, Pt 1–2 (ParteI) 89,90 (Milan) and Pt 7–8 (Parte II), 221–231 (Italian) BXX.
Lacombe, C., Prome, D., Blonquit, Y., Bardakdjian, J., Arous, N., Mrad, A., Prome, J-C., and Rosa, J. (1990) New results of hemoglobin variants structure determination by FAB-mass spectrometry. Hemoglobin 14, 529–548. BXM.
Green, B. N., Oliver, R. W. A., Falick, A. M., Shackleton, C. H. L., Roitman, F., and Witkowska, H. E. (1990) Electrospray MS, LSIMS for the rapid detection and characterisation of variant haemoglobins, in Biological Mass Spectrometry (Burlingame, A. L. and McCloskey, J. A., eds.), Elsevier, Amsterdam, pp. 129–146. XXX.
Hillenkamp, F., Karas, M., Ingendoh A., and Stahl, B. (1990) Matrix assisted UV-laser desorptton/ionization: A new approach to mass spectrometry of large biomolecules, in Biological Mass Spectrometry (Burlingame, A. L. and McCloskey, J. A., eds.), Elsevier, Amsterdam, pp. 49–60. XXX.
Pucci, P., Ferranti, P., Malorni, A., and Marino, G. (1990) FAB-MS analysis of haemoglobin variants’ use of V-8 protease in the identification of HbM Hyde Park and Hb San Jose. Biomed Environ. Mass Spectrom. 19, 568–572. XCM.
Falick, A. M., Shackleton, C. H. L., Green, B. N., and Witkowska, H. E. (1990) Tandem mass spectrometry in the clinical analysis of variant hemoglobins. Rapid Commun. Mass Spectrom. 4, 396–400. XXM.
Williamson, D., Nutkins, J., Rosthoj, S., Brennan, S. O., Williams, D. H., and Carrell, R. W. (1990) Characterisation of Hb Aalborg, a new unstable hemoglobin variant, by FAB mass spectrometry. Hemoglobin 14, 137–145. XCM.
Hill, R. E. (1990) The widening horizons of bioanalytical mass spectrometry. Clin. Chim. Acta. 194, 1–17. XXM.
Cappiello, A., Palma, P., Papayannopoulos, A, and Biemann, K. (1990) Efficient introduction of HPLC fractions into a high performance tandem mass spectrometer. Chromatographia 30, 477–483. BCX.
Frigeri, F., Pandolfi, G., Camera, A., Rotoli, B., Ferranti, P., Malorni, A, and Pucci, P. (1990) Hemoglobin G San-Jose: identification by mass spectrometry. Clin. Chem. Enzym. Comm. 3, 289–294. XXX.
Shackleton, C. H. L., Falick, A. M., Green, B. N., and Witkowska, H. E. (1991) Electrospray MS in the clinical diagnosis of variant haemoglobins. J. Chromatogr. 562, 175–190. XCM.
Falick, A. M., Witkowska, H. E., Labin, B. H., Nagel, R. L., and Shackleton, C. H. L (1991) Identification of variant haemoglobins by tandem mass spectrometry, in Techniques in Protein Chemistry II (Villafranca, J. J., ed.), Academic, San Diego, CA, pp. 557–565. XXX.
Oliver, R. W. A. and Green, B. N. (1991) On the application of electrospray-mass spectrometry to the characterisation of abnormal or variant haemoglobins. Trends. Anal. Chem. 10, 85–91. XXX.
Ferranti, P., Malorni, A., Pucci, P., Fanali, S., Nardi, A., and Ossicini, L. (1991) Capillary zone electrophoresis and mass spectrometry for the characterization of genetic variants of human hemoglobin. Anal. Biochem. 194, 1–8. XCM.
Matsuda, H., Matsuo, T., Katakuse, I., and Wada, Y. (1991) Investigation of amino acid mutations by high resolution mass spectrometry, in Mass Spectrometry of Peptides (Desiderio, D. M., ed.), CRC, Boca Raton, FL, pp. 221–256. XXX.
Lee, T. D. and Rahbar, S. (1991) The mass spectral analysis of hemoglobin variants, in Mass Spectrometry of Peptides (Desiderio, D. M., ed.), CRC, Boca Raton, FL, pp. 257–274. XXX.
Prome, D., Blouquit, Y., Ponthus, C., Prome, J. C., and Rosa, J. (1991) Structure of the human adult hemoglobin minor fraction Alb by electrospray and S.I.M.S. Pyruvic acid as amino-terminal blocking group. J. Biol. Chem. 266, 13,050–13,054. BCM.
Covey, T. R., Huang, E. C., and Henion, J. D. (1991) Structural characterization of protein tryptic peptides via liquid chromatography/MS and collision-induced dissociation of their doubly charged molecular ions. Anal. Chem. 63, 1193–1200. BCM.
Jensen, O. N., Hojrup, P., and Roepstorff, P. (1991) Plasma desorption mass spectrometry as a tool in characterization of abnormal proteins: Application to variant human hemoglobins. Anal. Biochem. 199, 175–183. XCM.
Johansson, I. M., Huang, E. H., Henion, J. D., and Zweigenbaum, J. (1991) Capillary electrophoresis atmospheric pressure ionization mass spectrometry for the characterizatfion of peptides. J. Chromatogr. 554, 311–327. BCM.
Oliver, R. W. A. (1991) LC and MS in the diagnosis of haemoglobin disorders. Lab. Equip. Dig. 29, 9–11. XXX.
Marsh, G., Masino, G., Pucci, P., Ferranti, P., Malorni, A., Kaeda, J., Marsh, J., and Luzzatto, L. (1991) A third instance of the high oxygen affinity variant, Hb Heathrow [β103(G5)Phe → Leu] identification of the mutation by mass spectrometry and by DNA analysis. Hemoglobin 15, 43–51. XXM.
Petrilli, P., Sepe, C., and Pucci, P. (1991) A new procedure for peptide alignment in protein sequence determination using FAB mass spectral data. Biol. Mass Spectrom. 20, 115–120. XCX.
Jensen, O. N. and Roepstorff, P. (1991) Application of reversed phase high performance liquid chromatography and plasma desorption mass spectrometry for the characterisation of a hemoglobin variant. Hemoglobin 15, 497–507. XXM.
Jensen, O. N., Roepstorff, P., Rozynov, B., Horanyi, M., Szelenyi, J., Hollan, S. R., Aseeva, E. A., and Spivak, V. A. (1991) Plasma desorption mass spectrometry of haemoglobin tryptic peptides for the characterisation of a Hungarian α-chain variant. Biol. Mass Spectrom. 20, 579–584. BXM.
Imai, K., Fushitani, K., Miyazaki, C. J., Ishimori, K., Kitagawa, T., Wada, Y., Morimoto, H., Morishima, I., Shih, D. T-b., and Tame, J. (1991) Site-directed mutagenesis in haemoglobin. J. Mol. Biol. 218, 769–778. XXX.
Witkowska, H. E., Lubin, B. H., Beuzard, Y., Baruchel, S., Esseltine, D. W., Vishinsky, E. P., Kleman, K. M., Bardakjian-Michau, J., Pinkoski, L., Cahn, S., Roitman, E., Green, B. N., Falick, A. M., and Shackleton, C. H. L. (1991) Sickle cell disease in a patient with sickle cell trait and compound heterozygosity for hemoglobin S and hemoglobin Quebec-Chori. N. Engl. J. Med. 325, 1150–1154. XXX..
Prome, J. C. (1991) Characterisation of post-translational modifications of proteins by mass spectrometry some selected problems. Analusis 19, 79–84. BCX.
Manning, L. R., Morgan, S., Beavis, R. C., Chait, B. T., Manning, J. R., Hess, J. R., Cross, M., Currell, D. L., Marini, M. A., and Winslow, R. B. (1991) Preparation, properties and plasma retention of human hemoglobin derivatives, comparison of uncrosslinked carboxymethylated hemoglobin with crosslinked tetrameric hemoglobin. Proc. Natl. Acad. Sci. USA 88, 3329–3333. BCM.
Goldberg, D. E., Slater, A. F. G., Beavis, R., Chait, B., Cerami, A., and Henderson, G. B. (1991) Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum, a catabolic pathway initiated by a specific aspartic protease. J. Exp. Med. 173, 961–969. BCM.
Lubin, B. H., Witkowska, H. E., and Kleman, K. (1991) Laboratory diagnosis of hemoglobinopathies. Clin. Biochem. 24, 363–374. XXM.
Chowdhury, S. K., Katta, V., and Chait, B. T. (1991) Electrospray ionization mass spectrometric analysis of proteins, in Methods and Mechanisms for Producing Ions from Large Molecules (Standing, K. G. and Ens, W., eds.), Plenum, New York (NATO Advanced Science Institute, Series B, vol. 269), pp. 201–210. XCX.
Ishimori, K., Imai, K., Miyazaki, G., Kitagawa, T., Wada, Y., Morimoto, H., and Morishima, I. (1992) Site-directed mutagenesis in hemoglobin. Biochemistry 31, 3256–3264. XXX.
Brennan, O., Shaw, J., Allen, J., and George, P. M. (1992) Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-Coventry but is replaced by a novel amino acid of mass 129 daltons. Br. J. Haematol. 81, 99–103. XCM.
Wada, Y. (1992) Mass spectrometry in the integrated strategy for the structural analysis of protein variants. Biol Mass Spectrom. 21, 617–624. XXX.
De Caterina, M., Esposito, P., Grimaldi, E., Di Mario, G., Scopacasa, F., Ferranti, P., Parlapiano, A., Malorni, A., Pucci, P., and Marino, G. (1992) Characterization of hemoglobin Lepore variants by advanced mass spectrometric procedures. Clin. Chem. 38, 1444–1448. XXM.
Ferrige, A. G., Seddon, M. J., Green, B. N., Jarvis, S. A., and Skilling, J. (1992) Disentangling electrospray spectra with maximum entropy. Rapid Commun. Mass Spectrom. 6, 707–711. XXX
Wada, Y., Matsuo, T., Papayannopoulos, I. A., Costello, C. E., and Biemann, K. (1992) Fast atom bombardment and tandem mass spectrometry for the characterisation of hemoglobin variants including a new variant. Int. J. Mass Spectrom. Ion Processes 122, 219–229. BCX.
De Angioletti, M., Maglione, G., Ferranti, P., De Bonis, C., Lacerra, G., Scarallo, A., Pagano, L., Fioretti, G., Cutolo, R., Malorni, A., Pucci, P., and Carestia, C. (1992) Hemoglobin City of Hope in Italy. Association of the gene with haplotype IX. Hemoglobin 16, 27–34. XCM.
Wada, Y., Tamura, J., Musselman, B. D., Kassel, D. B., Sakurai, T., and Matsuo, T. (1992) Electrospray ionization mass spectra of hemoglobin and transferrin by a magnetic sector mass spectrometer. Rapid Commun. Mass Spectrom. 6, 9–13. BCM.
Rotoli, B., Camera, A., Fontana, R., Frigeri, F., Pandolfi, G., Vecchione, R., Poggi, V., Longo, G., Carestia, C., De Angiolestti, M., Lacerra, G., Pucci, P., Marino, G., Ferranti, P., Malorni, A., Romano, R., and Formisano, S. (1992) Hb-Hyde Park. A de novo mutation identified by mass spectrometry and DNA analysis. Haematologica 77, 110–118. XXM.
Vassaur, C., Blouquit, Y., Kister, J., Prome, D., Kavanaugh, J. S., Rogers, P. H., Guillemin, C., Arnone, A., Galacteros, F., Poyart, C., Rosa, J., and Wajcman, H. (1992) Hemoglobin Thionville. J. Biol Chem. 267, 12,682–12,691 XXX.
Coghlan, D., Jones, G., Denton, K. A., Wilson, M. T., Chan, B., Harris, R., Woodrow, J. R., and Ogden, J.E. (1992) Structural and functional characterisation of recombinant human, haemoglobin A expressed in Saccharomyces cerevisiae. Eur. J. Biochem. 207, 931–936. XXX
Malorni, A., Pucci, P., Ferranti, P., and Marino, G. (1992) Characterisation of human hemoglobin variants by mass spectrometry, in Mass Spectrometry in the Biological Sciences: A Tutorial (Gross, M. L., ed.), Kluwer, Dordrecht, Germany, pp. 325–332. CBX.
Suwanrumpha, S., McClean, M. A., Fink, S. W., Wilder, C., Stachowiak, K., Dyckes, D. F., and Freas, R. B. (1992) Determination of biomolecules by using liquid chromatography and thermospray mass spectrometry, in Mass Spectrometry in the Biological Sciences: A Tutorial (Gross, M. L., ed.), Kluwer, Dordrecht, Germany, pp. 281–301. XXX.
Roepstorff, P. (1992) Plasma desorption mass spectrometry, principles and applications to protein studies, in Mass Spectrometry in the Biological Sciences: A Tutorial (Gross, M. L., ed.), Kluwer, Dordrecht, Germany, pp. 213–227. XXX.
Seta, K., Hail, M., Mylchreest, I., and Okuyama, T. (1992) Structural analysis of hemoglobin variant by microbore column HPLC/ESI/TSQMS. Kuromatogurafi 13, 349,350 (Japanese) XCX.
Mosca, A., Paleari, R., Rubino, F. M., Zecca, L., De Bellis, G., Debernardi, S., Baudo, F., Cappellini, D., and Fiorelli, G. (1993) Hemoglobin Abrusso identified by mass spectrometry and DNA analysis. Hemoglobin 17, 261–268. XCM.
Witkowska, H. E., Bitsch, F., and Shackleton, C. H. L. (1993) Expediting variant hemoglobin characterization by combined HPLC/electrospray mass spectrometry. Hemoglobin 17, 227–242. XXM.
Light-Wahl, K. J., Loo, J. A., Edmonds, C. G., Smith, R. D., Witkowska, H. E., Shackleton, C. H. L., and Wu, C. S. C. (1993) Collisionally activated dissociation and tandem mass-spectrometry of intact hemoglobin beta-chain variant proteins with electrospray ionization. Biol. Mass Spectrom. 22, 112–120. BCM.
Shen, T-J., Ho, N. T., Simplaceanu, V., Zou, M., Green, B. N., Tam, M. F., and Ho, C. (1993) Production of unmodified human adult hemoglobin in Escherichia coli. Proc. Natl. Acad. Sci 90, 8108–8112. BCM
Lane, P. A., Witkowska, H. E., Falick, A. M., Houston, M. L., and McKinna, J. D. (1993) Hemoglobin D Ibadan-beta thalassemia. detection by neonatal screening and confirmation by electrospray ionization mass spectrometry. Am. J. Hematol. 44, 158–161. XXM.
Brennan, S. O., Shaw, J. G., George, P. M., and Huisman, T. H. J. (1993) Posttranslational modification of beta 141 Leu associated with the β(75)Leu → Pro mutation in hemoglobin Atlanta. Hemoglobin 17, 1–7 XCM.
Ferranti, P., Parlapiano, A., Malorni, A., Pucci, P., Marino, G., Cossu, G., Manta, L., and Masala, B. (1993) Hemoglobin Oziero: a new alpha chain variant (α(71) Ala → Val) characterization using FAB-and electrospray-mass spectrometric techniques. Biochim. Biophys. Acta. 1162, 203–208. BCM.
De Llano, J. J. M., Jones, W., Schneider, K., Chait, B. T., Benjamin, L. J., and Weksler, B. (1993) Biochemical and functional properties of recombinant human sickle hemoglobin expressed in yeast. J Biol. Chem. 268, 27,004–27,011 XCX.
Wilson, J. B., Brennan, S. O., Allen, J., Shaw, J. G., Gu, L-H., and Huisman, T. H. J. (1993) The M gamma chain of human fetal hemoglobin is an A gamma chain with an in vitro modification of gamma 141 leucine to hydroxyleucine. J. Chromatogr. Biomed. Appl. 617, 37–42. XCM.
De Llano, J. J. M., Schneewind, O., Stetler, G., and Manning, J. M. (1993) Recombinant human sickle hemoglobin expressed in yeast. Proc. Natl. Acad. Sci. USA 90, 918–922. BCM.
Li, Y-T., Hsieh, Y.-L, Henion, J. T., and Ganem, B. (1993) Studies on heme binding in myoglobin, hemoglobin and cytochrome C by ion spray mass spectrometry. J. Am. Soc. Mass Spectrom. 4, 631–637. XXX.
Loo, J. A., Ogorzalek-Loo, R. R., and Andrews, P. C. (1993) Primary to quaternary protein structure determination with electrospray ionization and magnetic sector mass spectrometry. Org. Mass Spectrom. 28, 1640–1649. XXX.
Ganem, B. and Hemon, J. D. (1993) Detecting non-covalent complexes of biological macromolecules: new applications of ion-spray mass spectrometry. Chemiracts. Org. Chem. 6, 1–22. XXX.
Wajcman, H., Kalmes, G., Groff, P., Prome, D., Riou, J., and Galacteros, F. (1993) Hemoglobin Melusine, (α( 114)Pro → Ser) A new neutral hemoglobin variant. Hemoglobin 17, 397–405. XXX.
Wajcman, H., Kister, J., Prome, D., Galacteros, F., and Gilsanz, F. (1993) Hb Villaverde (β(89)Ser → Thr): the structural modification of an intrasubunit contact is responsible for a high oxygen affinity. Biochim. Biophys. Acta. 1225, 89–94. BCM.
Springer, D. L., Bull, R. J., Goheen, S. C., Sylvester, D. M., and Edmonds, C. G. (1993) Electrospray ionisation mass spectrometric characterization of acrylamide adducts to hemoglobin. J. Toxicol. Environ. Health 40, 161–176. XCM.
Bergmark, E., Calleman, C. J., He, F., and Costa, L. G. (1993) Determination of hemoglobin adducts in humans occupationally exposed to acrylamide. Toxicol. Appl. Pharmacol. 120, 45–54. XXM.
Shackleton, C. H. L. and Witkowska, H. E. (1994) Mass spectrometry in the characterisation of variant hemoglobins, in Mass Spectrometry Clinical and Biomedical Applications, vol 2 (Desiderio, D. M., ed.), Plenum, New York, pp. 135–199. XXX.
Wada, Y. and Matsuo, T. (1994) Structure determination of aberrant proteins, in Biological Mass Spectrometry, Present and Future (Matsuo, T., Caprioli, R. M., Gross, M. L., and Seyama, Y., eds.), Wiley, Chichester, UK, pp. 369–399. XXX.
Light-Wahl, K. L., Schwartz, B. L., and Smith, R. D. (1994) Observations on the non covalent quaternary associations of proteins by electrospray ionisation mass spectrometry. J. Am. Chem. Soc. 116, 5271–5278. BCX.
De Llano, J. J. and Manning, J. M. (1994) Properties of a recombinant hemoglobin double mutant. Protein Sci. 3, 1206–1212. BCM.
Yanase, H., Cahill, S., De Llano, J. J., Manning, L. R., Schneider, K., Chatt, B. T., Vandegriff, K. D., Winslow, R. M., and Manning, J. M. (1994) Properties of a recombinant hemoglobin with aspartic acid 99 (beta) substituted by lysine. Protein Sci. 3, 1213–1223. BCM
Wajcman, H., Kister, J., M’Rad, A., Soummer, A. M., and Galacteros, F. (1994) Hemoglobin Cemenelum: α(92)Arg → Trp) a hemoglobin variant of the alpha 1/beta 2 interface that displays a moderate increase in oxygen affinity. Ann. Hematol. 68, 73–76. XXX.
Bakhtiar, R., Wu, Q., Hofstadler, S. A., and Smith, R. D. (1994) Charge state specific facile gas-phase cleavage of Asp 75-Met 76 peptide bond in the alpha chain of human apohemoglobin probed by electrospray ionization mass spectrometry. Biol. Mass Spectrom 23, 707–710. BCM.
Ferranti, P., Malorni, A., and Pucci, P. (1994) Structural characterisisation of hemoglobin variants using capillary electrophoresis and fast atom bombardment mass spectrometry. Methods Enzymol. 231, 45–65. XXM.
Ishimori, K., Hashimoto, M., Imai, K., Fushitani, K., Miyazaki, G., Morimoto, H., Wada, Y., and Morishima, I. (1994) Sate directed mutagenesis in hemoglobin. Biochemistry 33, 2546–2553. XXM.
Konishi, Y. and Feng, R. (1994) Conformational stability of heme proteins in vacuo. Biochemistry 33, 9706–9711. BCM.
Bonaventura, C., Bonaventura, J., Stevens, R., and Millington, D. (1994) Acrylamide in polyacrylamide gels can modify proteins during electrophoresis. Anal. Biochem. 222, 44–48. BXX.
Rao, M. J., Schneider, K., Chatt, B. T., Chao, T. L., Keller, H., Anderson, S., Manjula, B. N., Kumar, R., and Acharya, A. S. (1994) Recombinant hemoglobin A produced in transgenic swine: structural equivalence with human hemoglobin A. Art Cells Blood Subs Immob. BioTech. 22, 695–770. BCM
Woolfit, A. R. and Bott, P. A. (1994) The analysis of native protein complexes by electrospray ionisation on an Autospec. Fisons Instruments Application Notes no. 36. XXX.
Kluger, R. and Song, Y. (1994) Changing a protein into a general acylating reagent. J. Org. Chem. 59, 733–736. BXX.
Ferranti, P., Barone, F., Pucci, P., Malorni, A., Marino, G., Pilo, G., Manta, L., and Masala, B. (1994) HbF-Sassari-a novel G-gamma variant with Thr at (75), characterised by MS techniques. Hemoglobin 18, 307–315. BCM.
Gilbert, S C., Van Urk, H., Greenfield, A. J., McAvoy, M. J., Denton, K. A., Coghlan, D., Jones, B. D., and Mead, D. J. (1994) Increase in copy number of an integrated vector during continuous culture of Hansenula polymorpha expressing functional human hemoglobin. Yeast 10, 1569–1580. BCM.
Kim, H-W., Shen, T-J., Sun, D. P., Ho, N. T., Madrid, M., and Ho, C. (1995) A novel low oxygen affinity recombinant hemoglobin (α(96) Val → Trp). J. Mel. Biol. 248, 867–882. XXX.
Shimizu, A. and Nakanishi, T. (1995) Applications of mass spectrometry for clinical laboratory test. Rinsho Byori. 43, 8–18. (Japanese) XXM.
Yanase, H., Manning, L. R., Vandegriff, K., Winslow, R. M., and Manning, J. M. ( 1995) A recombinant human hemoglobin with asparagnine-102(β) substituted by alanine has a limiting low oxygen affinity, reduced marginally by chloride. Protein Sci. 4, 21–28. BCM.
Hofstadler, S. A., Swanek, F. D., Gale, D. C., Ewing, A. G., and Smith, R. D. (1995) Capillary electrophoresis-electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 67, 1477–1480. XCM.
Prome, D., Prome, J. C., Gale, D. C., and Rosa, J. (1995) Characterization of new amino-terminal blocking groups in the normal human adult hemoglobin. Eur. Mass Spectrom. 1, 195–201. XCM.
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Oliver, R.W.A., Carrier, M.P. (1996). The Use of Databases in Searching the Literature of Biological Mass Spectrometry. In: Chapman, J.R. (eds) Protein and Peptide Analysis by Mass Spectrometry. Methods in Molecular Biology™, vol 61. Humana Press. https://doi.org/10.1385/0-89603-345-7:295
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