| Abstract: | ![]()
The sequences of 13 tryptic peptides of cow ?A-casein (accounting for about one half of the amino acid residues present in the protein) were established. The rennin sensitive linkage could be located in a large fragment (36 residues). ?-casein consists of a hydrophilic part (?-caseino-glycopeptide) and of a hydrophobic moiety (para-?-casein); in this latter, however, several quite hydrophilic sequences were characterized. Another feature of the ?-casein structure is the frequent duplication or triplication of certain amino acids (Pro-Pro; Phe-Phe; Gln-Gln-Gln-Asn-Glu-Glu-Glu; Pro-Pro-Lys-Lys-Asn-Gln-; etc. …). |
