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Sulphydryl and disulphide groups in casein

Published online by Cambridge University Press:  01 June 2009

G. M. Wallace  and
K. R. Aiyar
G. M. Wallace
Affiliation:
Food Technology Department, Massey University, Palmerston North, New Zealand
K. R. Aiyar
Affiliation:
Food Technology Department, Massey University, Palmerston North, New Zealand
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Summary

The method of Gaitonde (1967) was adapted for the measurement of cysteine and cystine in acid hydrolysates. Analysis of 3 different casein preparations indicated the presence of both cysteine and cystine in whole casein in the proportions of 1:1 by weight and in the molecular ratio of 2:1. If all the cysteine and cystine is associated with κ-casein then it appears that one mole of the latter contains 2 moles of cysteine and 1 mole of cystine. The sulphydryl group in whole casein appears not to be highly labile.

Type
Original Articles
Information
Journal of Dairy Research , Volume 36 , Issue 1 , February 1969 , pp. 115 - 123
Copyright
Copyright © Proprietors of Journal of Dairy Research 1969

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References

REFERENCES

Beeby, R. (1964). Biochim. biophys. Acta 82, 418.CrossRefGoogle Scholar
Benesch, R. E. & Benesch, R. (1958). J. Am. chem. Soc. 80, 1666.CrossRefGoogle Scholar
Block, R. J. & Bolling, D. (1940). The Determination of Amino Acids, p. 24. Minneapolis Minn.: Burgess Publ. Co.Google Scholar
Block, R. J. & Bolling, D. (1945). In The Amino Acid Composition of Proteins and Foods, chap. III, p. 142. Springfield, III.: C. C. Thomas.Google Scholar
Cecil, R. (1963). In The Proteins, vol. I, pp. 459, 388. (Ed. Neurath, H..) New York and London: Academic Press Inc.Google Scholar
Christ, W. (1956). Milchwissenschaft 11, 381.Google Scholar
Davidson, B. E. & Hird, F. J. R. (1967). Biochem. J. 104, 473.CrossRefGoogle Scholar
Deutsch, H. F. & Morton, J. I. (1958). J. biol. Chem. 231, 1107.CrossRefGoogle Scholar
Gaitonde, M. K. (1967). Biochem. J. 104, 627.CrossRefGoogle Scholar
Gordon, W. G., Semelt, W. F., Cable, R. S. & Morris, M. (1949). J. Am. chem. Soc. 71, 3293.CrossRefGoogle Scholar
Gordon, W. G. & Whittier, E. O. (1965). In Fundamentals of Dairy Chemistry, p. 54. (Eds. Webb, B. H. & Johnson, A. H..) Westport, Conn.: Avi Publ. Co.Google Scholar
Haurowitz, F. (1963). The Chemistry and Function of Proteins, 2nd ed. Chap. III, p. 25. New York and London: Academic Press Inc.Google Scholar
Hill, R. D. (1964). J. Dairy Res. 31, 285.CrossRefGoogle Scholar
Hipp, N. J., Basch, J J. & Gordon, W. G. (1961). Archs Biochem. Biophys. 94, 35.CrossRefGoogle Scholar
Hughes, W. L. (1947). J. Am. chem. Soc. 69, 1836.CrossRefGoogle Scholar
Jensen, E. V. (1959). In Sulphur in Proteins, p. 75. (Eds. Benesch, B., et al. ) New York: Academic Press Inc.Google Scholar
Jolles, P. (1966). Angew. chem. int. Ed. 5, 558.CrossRefGoogle Scholar
Kassel, B. & Brand, E. (1938). J. biol. Chem. 125, 435.CrossRefGoogle Scholar
Leach, S. J.(1966). In Laboratory Manual of Analytical Methods of Protein Chemistry, vol. IV, p. 3. (Eds. Alexander, P. & Lundgren, H. P..) Oxford: Pergamon Press Ltd.Google Scholar
Mckenzie, H. A. (1967). Adv. Protein Chem. 22, 123.Google Scholar
Mackinlay, A. G. & Wake, R. G. (1964). Biochim. biophys. Acta 93, 378.CrossRefGoogle Scholar
Madsen, N. B. & Cori, C. F. (1956). J. biol. Chem. 223, 1055.CrossRefGoogle Scholar
Nakai, S., Wilson, H. K. & Herreid, E. O. (1965). J. Dairy Sci. 48, 431.CrossRefGoogle Scholar
Swaisgood, H. E., Brunner, J. R. & Lillevik, H. A. (1964). Biochemistry, Easton 3, 1616.CrossRefGoogle Scholar
Waugh, D. F. (1961). J. phys. Chem., Ithaca 65, 1793.CrossRefGoogle Scholar
Waugh, D. F., Ludwig, M., Gillespie, J. M., Garner, J., Kleiner, E. S. & Noble, R. W. (1960). Fedn Proa. Fedn Am. Socs exp. Biol. 19, 337.Google Scholar
Waugh, D. F. & Von hippel, P. (1956). J. Am. chem. Soc. 78, 4576.CrossRefGoogle Scholar
Yoshino, U., Wilson, H. K. & Herreid, E. O. (1962). J. Dairy Sci. 45, 1459.CrossRefGoogle Scholar
Zweig, G. & Block, R. J. (1953). J. Dairy Sci. 36, 427.CrossRefGoogle Scholar