Abstract
Proteins occupy a unique status among the constituents of biological matter by virtue of their relatively large size and complex, multifaceted, and multireactive structures. These properties give them superb characteristics for functioning in biological systems in many different ways, but these characteristics also make many proteins susceptible to environmental stresses. While these susceptibilities to stresses are important in the functions of biological systems, allowing proteins to respond to or interact with the many constituents in biological systems, they are also easily attacked by a variety of chemicals and are subject to many deteriorative reactions. Indeed, susceptibility to and interaction with the environment by proteins are what make proteins highly important constituents that fulfill a major requirement for living things, namely, response to environment.
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
AALBERSE, R.C., DIEGES, P.H., KNUL-BRETLOVA, V., VOOREN, P., and AALBERSE, M. 1983A. IgG4 as a blocking antibody. Clin. Rev. Allergy 2, 289–;301.
AALBERSE, R.C., VAN DER GAAG, R., and VAN LEEUWEN, J. 1983B. I. Prolonged immunization results in an IgG4-restricted response. J. Immunol. 130, 722–726.
ACHARYA, A.S., and MANNING, J.M. 1980. Amadori rearrangement of glyceral-dehyde-hemoglobin Schiff base adducts. A new procedure for the determination of keto-amine adducts in proteins. J. Biol. Chem. 255, 7218–7224.
ACHARYA, A.S., and MANNING, J.M. 1981. Croos-linking of proteins with glycoaldehye. Fed. Proc., Fed. Am. Soc. Exp. Biol. 40 (6), 1613 (Abstr. 423).
BAILEY, A.J., and ROBINS, S.P. 1973. Development and maturation of the cross-links in the collagen fibres of skin. Front. Matrix Biol. 1, 130–156.
BENISEK, W.F., OGEZ, J.R., and SMITH, S.B. 1982. Design of site-specific pharmacologic reagents. Illustration of some alternative approaches by reagents directed towards steroid-hormone-specific targets. Adv. Chem. Ser. 198, 267–323.
BOHAK, Z. 1964. N-(DL-2-amino-2-carboxyethyl)-L-lysine, a new amino acid formed on alkaline treatment of proteins. J. Biol. Chem. 239, 2878–2887.
BOOKCHIN, R.M., and GALLOP, P.M.. 1968. Structure of hemoglobin Alc:Nature of the N-terminal /3-chain blocking group. Biochem. Biophys. Res. Commun. 32, 86–93.
BREW, K., CASTELLINO, F.J., VANAMAN, T.C., and HILL, R.L. 1970. Complete amino acid sequence of bovine a-lactalbumin. J. Biol. Chem. 245, 4570–4582.
CABACUNGAN, J.C., AHMED, A.I., and FEENEY, R.E. 1982. Amine boranes as alternative reducing agents for reductive alkylation of proteins. Anal. Biochem. 124, 272–278.
CANFIELD, R. 1963. The amino acid sequence of egg white lysozyme. J. Biol. Chem. 238, 2698–2707.
CANFIELD, R., and LIU, A.K. 1965. The disulfide bonds of egg white lysozyme (muramidase). J. Biol. Chem. 240, 1997–2002.
DAKIN, H.D. 1912. The racemization of proteins and their derivatives resulting from tautomeric change. Part I. J. Biol. Chem. 13, 357–362.
DIXON, H.B.F. 1972. A reaction of glucose with peptides. Biochem. J. 129, 203–208.
ERIKSSON, C. (Editor) 1981. Maillard Reactions in Food. Pergamon Press, Oxford.
ETIEVANT, M, LELUC, B., BOUCLIER, R., and HENOCQ, E. 1979. Immunoenzymatic study of IgG subclass specific for allergen in house dust immediate hypersensitivity. Ann. Allergy 43, 169–173.
FAGAN, D.L., SLAUGHTER, C.A, CAPRA, J.D., and SULLIVAN, T.J. 1982. Monoclonal antibodies to immunoglobulin G4 induce histamine release from human basophils in vitro. J. Allergy Clin. Immunol. 5, 399–404.
FEENEY, R.E. 1977. Chemical changes in food proteins. In Evaluation of Proteins for Humans. C.E. Bodwell (Editor). AVI Publishing Co., Westport, CT.
FEENEY, R.E., and WHITAKER, J.R. (Editors). 1982A. Modification of Proteins: Food, Nutritional, and Pharmacological Aspects, Adv. Chem. Ser. No. 198. American Chemical Society, Washington, DC.
FEENEY, R.E. and WHITAKER, J.R. 1982B. The Maillard reaction and its prevention. ACS Symp. Ser. 206, 201–229.
FEENEY, R.E., MACDONNELL, L.R., and DUCAY, E.D. 1956. Irreversible inacti- vation of lysozyme by copper. Arch. Biochem. Biophys. 61, 72–83.
FEENEY, R.E., ABPLANALP, H., CLARY, J.J., EDWARDS, D.L., and CLARK, J.R. 1963. A genetically varying minor protein constituent of chicken egg white. J. Biol. Chem. 238, 1732–1736.
FEENEY, R.E., BLANKENHORN, G., and DIXON, H.B.F. 1975. Carbonyl-amine reactions in protein chemistry. Adv. Protein Chem. 29, 135–203.
FEENEY, R.E., YAMASAKI, R.B., and GEOGHEGAN, K.F. 1982. Chemical modification of proteins: An overview. Adv. Chem. Ser. 198, 3–55.
FEENEY, R.E., OSUGA, D.T., MEARES, C.F., BABIN, D.R., and PENNER, M.H. 1983. Studies on iron-binding sites of transferrin by chemical modification. In Structure and Function of Iron Storage and Transport Proteins. I. Urushizaki, P. Aisen, I. Listowsky, and J. W. Drysdale (Editors). Elsevier, Amsterdam.
GEOGHEGAN, K.F., DALLAS, J.L., and FEENEY, R.E. 1980. Periodate inactivation of ovotransferrin and human serum transferrin. J. Biol. Chem. 255, 11429–11434.
GERSHWIN, M.E., OSUGA, D.T., WONG, W.S.D, WHITAKER, J.R., and FEENEY, R.E. 1984. Unpublished data, Davis, CA.
GLAZER, A.N., DELANGE, R.J., and SIGMAN, D.S. 1975. Chemical Modification of Proteins: Selected Methods and Analytical Procedures. North-Holland/American Elsevier, Amsterdam.
GWYNN, C.M., SMITH, J.M., LEON, G.L., and STANWORTH, D.R. 1978. Role of IgG4 subclass in childhood allergy. Lancet 1, 910–911.
HASEGAWA, K., and IWATA, S. 1982. Gas chromatography-mass spectrometry of lysinoalanine and the related cross-linked amino acids in alkali-treated food proteins. Agric. Biol. Chem. 46, 2513–2520.
HAYASHI, T., and NAMIKI, M. 1980. Formation of two-carbon sugar fragment at an early stage of the browning reaction of sugar with amine. Agric. Biol. Chem. 44, 2575–2580.
HAYASHI, T., and NAMIKI, M. 1981. On the mechanism of free radical formation during browning reaction of sugars with amino compounds. Agric. Biol. Chem. 45, 933–939.
HIRS, C.H.W., and TIMASHEFF, S.N. (Editors) 1977. Methods in Enzymology, Vol. 47. Academic Press, NY.
HIRS, C.H.W., and TIMASHEFF, S.N. (Editors) 1983. Methods in Enzymology, Vol. 91. Academic Press, NY.
HOLMQUIST, W.R., and SCHROEDER, W.A. 1966. The in vitro biosynthesis of hemoglobin Aic. Biochemistry 5, 2504–2512.
HOSENEY, R.C. 1984. Functional properties of pentosans in baked foods. Food Technol. 38, 114–117.
HOSENEY, R.C., and FAUBION, J.M. 1981. A mechanism for the oxidative gelation of wheat flour water-soluble pentosans. Cereal Chem. 58, 421.
JENCKS, W.P. 1969. Catalysis in Chemistry and Enzymology. McGraw-Hill, NY.
KLINE, L., HANSON, H.L., SONODA, T.T., GEGG, J.E., FEENEY, R.E., and LINEWEAVER, H. 1951. Role of glucose in the storage deterioration of whole egg powder. III. Effect of glucose removal before drying on organoleptic, baking, and chemical changes. Food Technol. 5, 323–331.
KRAAL, B., and HARTLEY, B.S. 1978. Reactivity of amino groups in various complexes of the peptide chain elongation factor EF-Tu from Escherichia coli. A new method of competitive labelling using reductive methylation. J. Mol. Biol. 124, 551–564.
KURATA, M., KIKUGAWA, Y., KUWAE, T, KOYAMA, I., and TAKAGI, T. 1980. A new reductive modification of hen’s egg white lysozyme with pyridine-borane. Chem. Pharm. Bull. 28, 2274–2275.
LEE, H.S. SEN, L.C., CLIFFORD, A.J., WHITAKER, J.R., and FEENEY, R.E. 1979. Preparation and nutritional properties of caseins covalently modified with sugars. Reductive alkylation of lysines with glucose, fructose or lactose. J. Agric. Food Chem. 27, 1094–1098.
MASTERS, P.M., and FRIEDMAN, M. 1980. Amino acid racemization in alkali- treated food proteins-chemistry, toxicology, and nutritional consequences. ACS Symp. Ser. 123, 165–194.
MEANS, G.E., and FEENEY, R.E. 1968. Reductive alkylation of amino groups in proteins. Biochemistry 7, 2192–2201.
MEANS, G.E., and FEENEY, R.E. 1971. Chemical Modification of Proteins. Holden- Day, San Francisco, CA.
MIHARA, S., and SHIBAMOTO, T. 1980. Mutagenicity of products obtained from cysteamine-glucose browning model systems. J. Agric. Food Chem. 28, 62–66.
MILLER, J.A., GRAVALLESE, E., and BUNN, H.F. 1980. Nonenzymic glycosyla- tion of erythrocyte membrane proteins. Relevance to diabetes. J. Clin. Invest. 65, 896–901.
NAKAGAWA, T., STADLER, B.M., HEINER, D.C., SKVARIL, F, and DE WECK, A.L. 1981. Flow cytometric analysis of human basopil degranulation. II. De- granulation induced by anti-IgE, anti-IgG4 and the calcium ionophore A23187. Clin. Allergy 11, 21.
NAMIKI, M., and HAYASHI, T. 1983. A new mechanism of the Maillard reaction involving sugar fragmentation and free radical formation. ACS Symp. Ser. 215, 21–45.
NASHEF, A.S., OSUGA, D.T., LEE, H.S., AHMED, A.I., WHITAKER, J.R., and FEENEY, R.E. 1977. Effects of alkali on proteins. Disulfides and their products. J. Agric. Food Chem. 25, 245–251.
PARISH, W.E. 1971. Detection of reaginic and short-term sensitizing anaphylactic or anaphylactoid antibodies to milk in sera of allergenic and normal persons. Clin. Allergy 1, 369–380.
PARISH, W.E. 1981. The clinical relevance of heat-stable, short-term sensitizing anaphylactic IgG antibodies (IgG S-TS) and of related activities of IgG4 and IgG2. Br. J. Dermatol. 105, 223–231.
PENNER, M.H., YAMASAKI, R.B., OSUGA, D.T., BABIN, D.R., MEARES, C.F., and FEENEY, R.E. 1983. Comparative oxidations of tyrosines and methionines in transferrins: Human serum transferrin, human lactotransferrin, and chicken ovo- transferrin. Arch. Biochem. Biophys. 225, 740–747.
PEPYS, J., PARISH, W.E., STENIUS-AARNIALA, B., and WIDE, L. 1979. Clinical correlations between long-term (IgE) and short-term (IgG4 S-TS) anaphylactic antibodies in atopic and “nonatopic” subjects with respiratory allergic diseases. Clin. Allergy 9, 645–658.
PERELMUTTER, L. 1983. IgG4 and the immune system. Clin. Rev. Allergy 2, 267–287.
POLLOCK, G.E., CHENG, C.-N., and CRONIN, S.E. 1977. Determination of the D and L isomers of some protein amino acids present in soils. Anal. Chem. 49, 2–7.
POLLOCK, G.E., FEENEY, R.E, and WHITAKER, J.R. 1979. Unpublished data, Moffett Field and Davis, CA.
RAHBAR, S. 1968. An abnormal hemoglobin in red cells of diabetics. Clin. Chim. Acta 22, 296–298.
RAY, W.J, JR., and KOSHLAND, D.E, JR. 1962. Identification of amino acids involved in phosphoglucomutase action. J. Biol. Chem. 237, 2493–2505.
ROGERS, T.B, GOLD, R.A., and FEENEY, R.E. 1977. Ethoxyformylation and pho- tooxidation of histidines in transferrins. Biochemistry 16, 2299–2305.
SCHIFF, H. 1901. Trennung von Amin-und Saurefunction in Losungen von amin- sauren mittelst Formaldehyd. Justus Liebig’s Ann. Chem. 319, 59–76.
SCHOBERL, A, and RAMBACHER, P. 1939. Hydrolytic cleavage of the disulfide linkages in cystine derivatives, glutathione and insulin. Justus Liebigs. Ann. Chem. 538, 84–98.
SEN. L.C, GONZALES-FLORES, E, FEENEY, R.E, and WHITAKER, J.R. 1977. Reactions of phosphoproteins in alkaline solutions. J. Agric. Food Chem. 25, 632–638.
SHAKIB, F, and STANWORTH, D.R. 1979. IgG4: A possible mediator of anaphylaxis in a haemophiliac patient. Clin. Allergy 9, 597–603.
SHAKIB, F, McLAUGHLAN, P, STANWORTH, D.R, SMITH, E, and FAIRBURN, E. 1977. Elevated serum IgE and IgG4 in patients with atopic dermatitis. Br. J. Dermatol. 97, 59–63.
SHIBAMOTO, T. 1980. Mutagenicity of 1,5(or 7)-dimethy1-2,3,6,7-tetrahydro-1H,5H-bicyclopentapyrazine obtained from a cyclotene/NH3 browning model system. J. Agric. Food Chem. 28, 883–884.
SPINGARN, N.E, and GARVIE, C.T. 1979. Formation of mutagens in sugar-ammonia model systems. J. Agric. Food Chem. 27, 1319–1321.
STANWORTH, D.R. 1983. Immunochemical aspects of human IgG4. Clin. Rev. Allergy 2, 183–195.
STEVENS, V.J, ROUZER, C.A, MONNIER, V.M, and CERAMI, A. 1978. Diabetic cataract formation: Potential role of glycosylation of lens crystallins. Proc. Natl. Acad. Sci. U.S.A. 75, 2918–2922.
TODA, H, SEKIZAWA, J, and SHIBAMOTO, T. 1981. Mutagenicity of the L-rham- nose-ammonia-hydrogen sulfide browning reaction mixture. J. Agric. Food Chem. 29, 381–384.
TSOU, C.-L. 1962. Relation between modification of functional groups of proteins and their biological activity. 1. A graphical method for the determination of the number and type of essential groups. Sci. Sin. 11, 1535–1558.
VANAMAN, T.C., BREW, K., and HILL, R.L. 1970. Disulfide bonds of bovine a- lactalbumin. J. Biol. Chem. 245, 4583–4590.
WALLER, G.R., and FEATHER, M.S. (Editors) 1983. The Maillard Reaction in Foods and Nutrition, ACS Symp. Ser. No. 215. American Chemical Society, Washington, DC.
WEIL, L., GORDON, W.G., and BUCHERT, A.R. 1951. Photooxidation of amino acids in the presence of Methylene Blue. Arch. Biochem. Biophys. 33, 90–109.
WHITAKER, J.R., and FEENEY, R.E. 1983. Chemical and physical modification of proteins by the hydroxide ion. CRC Crit. Rev. Food Sei. Nutr. 19, (3), 173–212.
WHITAKER, J.R., and FUJIMAKI, M. (Editors) 1980. Chemical Deterioration of Proteins, ACS Symp. Ser. No. 123. American Chemical Society, Washington, DC.
WONG,W.S.D., OSUGA, D.T., and FEENEY, R.E. 1984A. Pyridine borane as a reducing agent for proteins. Anal. Biochem. 138, 58–67.
WONG,W.S.D., OSUGA, D.T., and FEENEY, R.E. 1984B. Determination of tryptophan as the reduced derivative by acid hydrolysis and chromatography. Anal Biochem. 143, 62–70.
WONG,W.S.D., OSUGA, D.T., and FEENEY, R.E. 1985A. 1-Deoxyglycitolation of protein amino groups and their regeneration by periodate oxidation. int. J. Peptide Protein Res. 26, 55–62.
WONG, W.S.D., OSUGA, D.T., WHITAKER, J.R, and FEENEY, R.E. 1985B. Inactivation of chicken egg white lysozyme and ovomucoid with copper. Manuscript in preparation.
WOODARD, J.C., and SHORT, D.D. 1975. Renal toxicity of N£-(DL-2-amino-2-car- boxyethyl)-L-lysine (lysinoalanine) in rats. Fed. Proc., Fed. Am. Soc. Exp. Biol. 34, 929 ( Abstr. No. 4022 ).
YAMASAKI, R.B., OSUGA, D.T., and FEENEY, R.E. 1982. Periodate oxidation of methionine in proteins. Anal. Biochem. 126, 183–189
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1985 AVI Publishing Co.
About this chapter
Cite this chapter
Feeney, R.E., Whitaker, J.R., Wong, W.S.D., Osuga, D.T., Gershwin, M.E. (1985). Chemical Reactions of Proteins. In: Richardson, T., Finley, J.W. (eds) Chemical Changes in Food during Processing. Basic Symposium Series. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2265-8_12
Download citation
DOI: https://doi.org/10.1007/978-1-4613-2265-8_12
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-9389-7
Online ISBN: 978-1-4613-2265-8
eBook Packages: Springer Book Archive