Hostname: page-component-848d4c4894-sjtt6 Total loading time: 0 Render date: 2024-07-07T04:57:24.143Z Has data issue: false hasContentIssue false
  • English
  • Français

The effect of reduction and alkylation on the primary phase of rennin action on unheated and heated milk

Published online by Cambridge University Press:  01 June 2009

G. A. Wilson ,
J. V. Wheelock  and
A. Kirk
G. A. Wilson
Affiliation:
School of Biological Sciences, The University, Bradford, Yorkshire, BD7 1DP
J. V. Wheelock
Affiliation:
School of Biological Sciences, The University, Bradford, Yorkshire, BD7 1DP
A. Kirk
Affiliation:
School of Biological Sciences, The University, Bradford, Yorkshire, BD7 1DP
Get access Rights & Permissions [Opens in a new window]

Summary

The effects of cystine-reducing and sulphydryl-alkylating agents on the extent of the primary phase of rennin action on unheated and heated milk samples were studied. Alkylating agents alone had a negligible effect, but heated samples, reduced with tri-n-butyl phosphine prior to alkylation with a mono-functional agent (sodium iodoacetate) did not show the usual inhibition of the primary phase. Heated samples, reduced and alkylated with a bi-functional agent (ethylene dibromide) which can re-cross-link the broken disulphide bonds, however, did give the normal inhibition. These results suggest that effects on the primary phase due to heat treatment of milk are determined to a large extent by rearrangement of the disulphide cross-links, and if these are permanently broken, heat appears to have little effect.

The results differ in some important respects from those obtained on the complex formed between isolated β-lactoglobulin and isolated κ-casein, and therefore throw doubt on the generally held view that there is a similar type of interaction in whole milk.

Type
Research Article
Information
Journal of Dairy Research , Volume 41 , Issue 1 , February 1974 , pp. 37 - 44
Copyright
Copyright © Proprietors of Journal of Dairy Research 1974

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

Brewer, C. F. & Riehm, J. P. (1967). Analytical Biochemistry 18, 248.CrossRefGoogle Scholar
Crewther, W. G., Dowling, L. M., Inglis, A. S. & Maclaren, J. A. (1967). Textile Research Journal 37, 736.CrossRefGoogle Scholar
Hill, R. D. (1969). Journal of Dairy Research 36, 409.CrossRefGoogle Scholar
Hill, R. D. (1970). Journal of Dairy Research 37, 187.CrossRefGoogle Scholar
Hindle, E. J. & Wheelock, J. V. (1970). Journal of Dairy Research 37, 389.CrossRefGoogle Scholar
Jocelyn, P. C. (1972). Biochemistry of the SH group, p. 141. London and New York: Academic Press.Google Scholar
Maclaren, J. A. & Sweetman, B. J. (1966 a). Australian Journal of Chemistry 19, 2347.CrossRefGoogle Scholar
Maclaren, J. A. & Sweetman, B. J. (1966 b). Australian Journal of Chemistry 19, 2365.CrossRefGoogle Scholar
Mattick, E. C. V. & Hallett, H. S. (1929). Journal of Agricultural Science 19, 452.CrossRefGoogle Scholar
Morrissey, P. A. (1969). Journal of Dairy Research 36, 333.CrossRefGoogle Scholar
Pofahl, T. R. & Vakaleris, D. G. (1968). Journal of Dairy Science 51, 1345.CrossRefGoogle Scholar
Sawyer, W. H. (1969). Journal of Dairy Science 52, 1347.CrossRefGoogle Scholar
Sawyer, W. H., Coulter, S. T. & Jenness, R. (1963). Journal of Dairy Science 46, 564.CrossRefGoogle Scholar
Smyth, D. G., Blumenfeld, O. O. & Konigsberg, W. (1964). Biochemical Journal 91, 589.Google Scholar
Tessier, H., Yaguchi, M. & Rose, D. (1969). Journal of Dairy Science 52, 139.CrossRefGoogle Scholar
Wilson, G. A. & Wheelock, J. V. (1972). Journal of Dairy Research 39, 413.CrossRefGoogle Scholar
Zittle, C. A., Thompson, M. P., Custer, J. H. & Cerbulis, J. (1962). Journal of Dairy Science 45, 807.CrossRefGoogle Scholar