JDS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Journal of Dairy Science Vol. 62 No. 2 195-203
© 1979 by American Dairy Science Association ®
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Doi, H.
Right arrow Articles by Kanamori, M.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Doi, H.
Right arrow Articles by Kanamori, M.

Heterogeneity of Reduced Bovine {kappa}-Casein

H. Doi, F. Ibuki and M. Kanamori

Department of Agricultural, Chemistry Kyoto Prefectural University, Shimogamo, Kyoto 606, Japan

ABSTRACT

The heterogeneity and some properties of {kappa}-casein were investigated, {kappa}-Casein preparations independently were prepared from milk from a single cow by the modified urea-sulfuric acid method and by the gel filtration method. The two preparations were fractionated by diethylaminoethyl-cellulose chromatography to one fraction, P-1, eluted with the front and 5 fractions, P-2 to P-6, eluted with increasing salt concentration. The amino acid compositions of P-2 to P-6 were identical, but fractions eluted with high salt concentrations had more carbohydrate (sialic acid, hexose, and hexosamine). Fractions P-2 to P-6 showed the same mobility on sodium dodecyl sulfate-electrophoresis, and their carboxyl-terminal residue was valine in all fractions. Each fraction showed a different mobility in disc gel electrophoresis containing urea, but the mobilities decreased to that of the slower moving fraction after treatment with neuraminidase. The micelle-stabilizing ability of each fraction was similar. In ultracentrifugal experiments, each fraction gave one peak and the sedimentation coefficients (s37) were between 17.5 s and 12.7 s. Intrinsic viscosity [{eta}] was similar at various temperatures. The values of s37 and [{eta}]37 indicate that each fraction associated and formed a polymer with a molecular weight of 50 x 104.




This article has been cited by other articles:


Home page
J DAIRY SCIHome page
H. M. Farrell Jr., R. Jimenez-Flores, G. T. Bleck, E. M. Brown, J. E. Butler, L. K. Creamer, C. L. Hicks, C. M. Hollar, K. F. Ng-Kwai-Hang, and H. E. Swaisgood
Nomenclature of the Proteins of Cows' Milk--Sixth Revision
J Dairy Sci, June 1, 2004; 87(6): 1641 - 1674.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1979 by the American Dairy Science Association ®.