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 HighWire Citing Articles via Google Scholar Google Scholar Articles by Groves, M. L. Articles by Jones, S. B. Search for Related Content PubMed PubMed Citation Articles by Groves, M. L. Articles by Jones, S. B.

TS-A², TS-B, R-, and S-Caseins: Their Isolation, Composition, and Relationship to the ß- and -Casein Polymorphs A² and B

Eastern Regional Research Laboratory, ¹ Philadelphia, Pennsylvania 19118

ABSTRACT

TS-A², R-, S-, and TS-B caseins are minor components of micellar caseins typed ß and -A² and B. Based on amino acid analysis, TS-A² and S-caseins form one pair of polymorphs and R- and TS-B another. The polymorphs in each pair differ only by a single amino acid substitution (Arg Ser) also found in the ß- and -variants. R- and TS-B are smaller than TS-A² and S-casein by two amino acids in the N-terminal portion of the molecule. These proteins have a molecular weight of about 12,000 and contain no phosphorus or cystine but have one residue of tryptophan. These findings, together with results of partial sequencing, support the hypothesis that the proteins have the same structure as the C-terminal portions of the ß- and -caseins.

¹ Agricultural Research Service, USDA.

This article has been cited by other articles:

				W. N. Marmer, P. Magidman, and H. M. Farrell JR Pyrolysis Gas Chromatography of Wool: Part II: Detection and Quantitation of Tryptophan in Wool and Simple Proteins Textile Research Journal, October 1, 1989; 59(10): 616 - 622. [Abstract] [PDF]