Hostname: page-component-cd9895bd7-gvvz8 Total loading time: 0 Render date: 2024-12-24T17:52:31.838Z Has data issue: false hasContentIssue false
  • English
  • Français

Reductive methylation of lysine residues in casein

Published online by Cambridge University Press:  01 June 2009

N. F. Olson ,
T. Richardson  and
J. G. Zadow
N. F. Olson
Affiliation:
Department of Food Science, University of Wisconsin, Madison, Wisconsin, U.S.A.
T. Richardson
Affiliation:
Department of Food Science, University of Wisconsin, Madison, Wisconsin, U.S.A.
J. G. Zadow
Affiliation:
Department of Food Science, University of Wisconsin, Madison, Wisconsin, U.S.A.
Get access Rights & Permissions [Opens in a new window]

Summary

The effect of reductive methylation on the properties of αs-, β- and κ-caseins was studied using preparations of these proteins in which 20 or 60% of the lysyl residues had been reductively methylated. This modification appeared to affect the physicochemical properties of the protein to an insignificant extent and in particular, electrophoretic mobility, sensitivity to precipitation by Ca2+ and solubility of Ca salts of individual proteins were only slightly altered. The use of caseins which had been subjected to methylation with radioactive formaldehyde is suggested as a potentially valuable method for the study of protein interactions.

Type
Original Articles
Information
Journal of Dairy Research , Volume 45 , Issue 1 , February 1978 , pp. 69 - 76
Copyright
Copyright © Proprietors of Journal of Dairy Research 1978

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

Aschaffenburg, R. (1963). Journal of Dairy Research 30, 259.CrossRefGoogle Scholar
Fleck, A. & Munro, H. N. (1965). Clinica chimica Acta 11, 2.CrossRefGoogle Scholar
Habeeb, A. F. S. A. (1966). Analytical Biochemistry 14, 328.CrossRefGoogle Scholar
Hill, R. D. & Craker, B. A. (1968). Journal of Dairy Research 35, 13.CrossRefGoogle Scholar
Lin, Y., Means, G. E. & Feeney, R. E. (1969). Journal of Biological Chemistry 244, 789.CrossRefGoogle Scholar
Means, G. E. & Feeney, R. E. (1968). Biochemistry 7, 2192.CrossRefGoogle Scholar
Moore, S., Cole, R. D., Gundlach, H. G. & Stein, W. H. (1958). Proceedings, 4th International Congress of Biochemistry 8, 52.Google Scholar
Noble, R. W. Jr & Waugh, D. F. (1965). Journal of the American Chemical Society 87, 2236.CrossRefGoogle Scholar
Ottesen, M. & Svensson, B. (1972). Comptes Rendus des Travauz du Laboratoire Carlsberg 38, 445.Google Scholar
Thompson, M. P., Kiddy, C. A., Johnston, J. O. & Weinberg, R. M. (1964). Journal of Dairy Science 47, 378.CrossRefGoogle Scholar
Zittle, C. A., Cerbulis, J., Pepper, L. & Della Monica, E. S. (1959). Journal of Dairy Science 42, 1897.CrossRefGoogle Scholar
Zittle, C. A. & Custer, J. H. (1963). Journal of Dairy Science 46, 1183.CrossRefGoogle Scholar