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Preparation and amino acid sequence of human kappa-casein.
Human kappa-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 kappa-casein was compared to those of goat, ewe, cow and rat kappa-caseins. Only 22% of the residues are identical in homologous positions. The rate of divergence of the 93-residue N-terminal segment (para-kappa-casein) appears to be higher than that of the rest of the molecule.
PMID: 4018271 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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Identification of a novel opioid peptide (Tyr-Val-Pro-Phe-Pro) derived from human alpha S1 casein (alpha S1-casomorphin, and alpha S1-casomorphin amide).
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[Biochem J. 1996]
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Characterization of three types of human alpha s1-casein mRNA transcripts.
Johnsen LB, Rasmussen LK, Petersen TE, Berglund L.
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[Biochem J. 1995]
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Characterization of bovine kappa-casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high-performance gel-permeation chromatography.
Vreeman HJ, Visser S, Slangen CJ, Van Riel JA.
Biochem J. 1986 Nov 15; 240(1):87-97.
[Biochem J. 1986]