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The role of lysine residues in the coagulation of casein

Published online by Cambridge University Press:  01 June 2009

R. D. Hill  and
Barbara A. Craker
R. D. Hill
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia
Barbara A. Craker
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia
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Summary

Coagulation of rennin-treated casein was inhibited by treatment of the casein with dimethylaminonaphthalene sulphonyl chloride. The effect was caused by substitution on lysine side chains of the κ-casein fraction, and inhibition was complete when 2–3 lysine residues/molecule were blocked. This level of substitution did not affect other properties of the κ-casein, such as the release from it of non-protein nitrogen (NPN) by rennin and its ability to stabilize αs-and β-caseins in the presence of Ca++. The evidence suggests that lysine side chains on κ-casein take part in the coagulation of rennin-treated casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 35 , Issue 1 , February 1968 , pp. 13 - 18
Copyright
Copyright © Proprietors of Journal of Dairy Research 1968

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References

REFERENCES

Gray, W. R. & Hartley, B. S. (1963). Biochem. J. 89, 59.CrossRefGoogle Scholar
Herskovits, T. T. & Mescanti, L. (1965). J. biol. Chem. 240, 639.CrossRefGoogle Scholar
Hill, R. D. & Hansen, R. R. (1963). J. Dairy Res. 30, 375.CrossRefGoogle Scholar
Hill, R. D. & Laing, R. R. (1965). J. Dairy Res. 32, 193.CrossRefGoogle Scholar
Hill, R. D. & Laing, R. R. (1967). Biochim. biophys. Acta 132, 188.CrossRefGoogle Scholar
Hoagland, P. D. (1966). J. Dairy Sci. 49, 783.CrossRefGoogle Scholar
Hsu, R. Y., Anderson, L., Baldwin, R. L., Ernstrom, C. A. & Swanson, A. M. (1958). Nature, Lond. 182, 798.CrossRefGoogle Scholar
Mcfarlane, A. S. (1938). Nature, Lond. 142, 1023.CrossRefGoogle Scholar
Swaisgood, H. E. & Brunner, J. R. (1963). J. Dairy Sci. 46, 596.Google Scholar
Woychik, J. (1966). Abstr. Pap. Am. chem. Soc. Sept. 1966, C226.Google Scholar
(Dairy Sci. Abstr. 29, [329].)Google Scholar
Zittle, C. A. & Custer, J. H. (1963). J. Dairy Sci. 46, 1183.CrossRefGoogle Scholar