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Structure primaire du caseinomacropeptide des caseines κ porcine et humaine
Author(s) -
Chobert Jean-Marc,
Mercier Jean-Claude,
Bahy Chantal,
Hazé Gérard
Publication year - 1976
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(76)80838-1
Subject(s) - amino acid , chymosin , chemistry , glycopeptide , biochemistry , peptide sequence , casein , microbiology and biotechnology , biology , gene , antibiotics
The amino acid sequence of porcine and human caseinomacropeptides (CMP), the C‐terminal glycopeptide released from κ‐casein by chymosin at the initial step of milk coagulation, have been investigated. The complete amino acid sequence of porcine CMP and that of the first 59 amino acid residues of human CMP have been determined. Porcine and human CMPs contain 71 and likely 65 amino acid residues respectively. The extra hexapeptide 38–43 found in porcine CMP arises obviously from the duplication of the DNA fragment coding for the 6 preceding amino acids.