Hostname: page-component-78c5997874-j824f Total loading time: 0 Render date: 2024-11-05T16:56:13.975Z Has data issue: false hasContentIssue false
  • English
  • Français

The effect of the modification of arginine side chains in casein on the coagulation of rennin-altered casein

Published online by Cambridge University Press:  01 June 2009

R. D. Hill
R. D. Hill
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia
Get access Rights & Permissions [Opens in a new window]

Summary

The modification of arginine residues in casein by treatment with glyoxal at pH 8·6 resulted in an inhibition of the coagulation of rennin-treated casein. The effective residues are on the κ-casein fraction and inhibition of coagulation was complete when about 1·5 residues of arginine/mole of κ-casein had been altered. It is suggested that the arginine forms part of a positively charged region that also includes lysine and histidine residues, and that this region is important in the coagulation of the casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 2 , June 1970 , pp. 187 - 192
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Bowes, J. H. & Cater, C. W. (1968). Biochim. biophys. Acta 168, 341.Google Scholar
Hill, R. D. & Craker, B. A. (1968). J. Dairy Res. 35, 13.Google 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.Google Scholar
Jollès, J., Alais, C. & Jollès, P. (1968). Biochim. biophya. Acta 168, 591.CrossRefGoogle Scholar
Mackinlay, A. G. & Wake, R. G. (1964). Biochim. biophys. Acta 93, 378.CrossRefGoogle Scholar
Macpherson, H. T. (1946). Biochem. J. 40, 470.CrossRefGoogle Scholar
Melnychyn, P. & Wolcott, J. M. (1967). J. Dairy Sci. 48, 780.Google Scholar
Nakaya, K., Horinishi, H. & Shibata, K. (1967). J. Biochem., Tokyo 61, 345CrossRefGoogle Scholar
Osterburg, R. (1961). Biochim. biophys. Acta 54, 424.Google Scholar
Reeves, R. E. & Latour, N. G. (1958). Science, N.Y. 128, 472.CrossRefGoogle Scholar
Williams, J. & Sanger, F. (1959). Biochim. biophys. Acta 33, 294.Google Scholar
Zittle, C. A. & Custer, J. H. (1963). J. Dairy Sci. 46, 183.Google Scholar