HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Nagasawa, T. Articles by Kuwahara, K. Search for Related Content PubMed PubMed Citation Articles by Nagasawa, T. Articles by Kuwahara, K.

Isolation of Canine _s-Casein and Major Whey Protein Component A and Their Amino Acid Composition

Central Research Laboratory, Morinaga Milk Industry Company, Ltd., Tokyo, Japan

ABSTRACT

Canine whole casein shows two strong bands designated "Canine _s- and ß-casein" corresponding to bovine _s- and ß-casein on gel electrophoresis, but both _s- and ß-casein have lower mobilities than bovine counterparts. Canine _s-casein was isolated by column chromatography on DEAE cellulose, whereas canine ß-casein fraction was isolated by urea fractionation. Phosphorus content and calcium sensitivity of the canine _s-casein and ß-casein fraction resemble those of bovine _s- and ß-casein, espectively. Canine _s-casein contains more arginine and less serine, glycine, methionine and lysine. Canine ß-casein fraction has a high nonpolar amino acid as bovine ß-casein, but it is low in glycine and tryptophan. Canine whey protein has five major bands on gel electrophoresis. Major Component A, the fastest moving band has greater mobility than bovine ß-lactoglobulin. Component A was isolated by salt fractionation and by column chromatography on DEAE cellulose. Amino acid composition of Component A resembles that of bovine ß-lactoglobulin, with less lysine and more arginine in the former. Also it resembles that of porcine ß-lactoglobulin, with less serine and lysine and more tyrosine and tryptophan in the former.