Open AccessStructure primaire de la caséine β bovine
Author(s) -
Ribadeaudumas Bruno,
Brig Ghislaine,
Grosclaude François,
Mercier JeanClaude
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb01389.x
Subject(s) - edman degradation , chemistry , peptide , casein , chromatography , sephadex , peptide sequence , amino acid , biochemistry , fractionation , enzyme , gene
All the expected tryptic and CNBr peptides from bovine β‐casein A 2 were previously isolated and analyzed [1]. The complete positioning of these peptides was reported later on [2]. The present report deals with the sequencing of 65 amino acid residues at the carboxyl‐terminus of β‐casein A 2 : ‐His‐Gln‐Pro‐His‐Gln‐Pro‐Leu‐Pro‐Pro‐Thr‐Val‐Met‐Phe‐Pro‐Pro‐Gln‐Ser‐Val‐Leu‐ Ser‐Leu‐Ser‐Gln‐Ser‐Lys‐Val‐Leu‐Pro‐Val‐Pro‐Glu‐Lys‐Ala‐Val‐Pro‐Tyr‐Pro‐Gln‐Agr‐Asp‐Met‐Pro‐Ile‐Gln‐Ala‐Phe‐Leu‐Leu‐Tyr‐Gln‐Gln‐Pro‐Val‐Leu‐Gly‐Pro‐Val‐Arg‐Gly‐Pro‐Phe‐Pro‐Ile‐Ile‐Val · OH. This result was obtained by using well known methods such as enzymic or chemical cleavages of the peptide chain, fractionation of peptides by Sephadex or Dowex column chromatography, paper electrophoresis or chromatography, and sequential Edman degradation. The carboxyl‐terminal tryptic peptide is very likely identical with a peptide isolated by Matoba et al. [3] from a tryptic digest of whole casein, and characterized by its bitter taste.