Open AccessStructure primaire de la caséine α s1 bovine
Author(s) -
Mercier JeanClaude,
Grosclaude François,
RibadeauDumas Bruno
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb01101.x
Subject(s) - edman degradation , exopeptidase , protein primary structure , chemistry , peptide sequence , phosphoprotein , sequence (biology) , amino acid , biochemistry , hydrolysis , stereochemistry , phosphorylation , gene
Earlier work in this laboratory on the determination of the primary structure of bovine α s1 casein [1–5] established that this phosphoprotein is composed of only one single peptide chain of 198 residues. The sequence of 101 residues have already been determined: the substitution of Glu/Gly at position 191 in the COOH‐terminal region differentiates the B and C genetic variants [1–3]. The sequence of 53 amino acid residues in the NH 2 ‐terminal region was also determined [5]. This publication deals with the sequence of the central part of the chain. Sequence determinations have been made on various tryptic [2], CNBr and chymotryptic [4] peptides obtained earlier, which have been further broken down with the help of endopeptidases or mild acid hydrolylysis into smaller fragments to which classical methods of degradation have been applied: exopeptidase hydrolysis and substractive Edman's degradation. The results obtained and previously published results establish the sequence of 172 amino acid residues in the molecule. The residues of which the positions have not been established so far are situated in 2 regions of the chain, between position 46 to 52 and position 61 to 77. These 2 regions are characterized by the presence of phosphorus and their sequences will be dealt with in our final publication.