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Preparation and amino acid sequence of human κ‐casein
Author(s) -
Brig Ghislaine,
Chtourou Abdessatar,
Ribadeau-Dumas Bruno
Publication year - 1985
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(85)80872-3
Subject(s) - residue (chemistry) , casein , chemistry , protein primary structure , biochemistry , peptide sequence , sequence (biology) , amino acid residue , chromatography , gene
Human κ‐casein was prepared from whole casein by successive hydroxyapatite and thiol‐Sepharose chromatographies. The primary structure of its 99‐residue N‐terminal fragment has been determined by sequencing peptides obtained by tryptic and chymotryptic digestions of the whole protein. This fragment overlaps the known sequence of the 65‐residue C‐terminal fragment. The 158‐residue sequence of human κ‐casein was compared to those of goat, ewe, cow and rat κ‐caseins. Only 22% of the residues are identical in homologous positions. The rate of divergence of the 93‐residue N‐terminal segment (para‐κ‐casein) appears to be higher than that of the rest of the molecule.