Human beta-casein. Amino acid sequence and identification of phosphorylation sites

The primary structure of human beta-casein has been determined by automated Edman degradation of the intact protein and of peptides derived therefrom by hydrolysis with trypsin and by chemical cleavage with cyanogen bromide. For each form of this multiphosphorylated protein (0-5 P/molecule), phospho...

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Bibliographic Details
Published in:The Journal of biological chemistry 1984-04, Vol.259 (8), p.5132-5138
Main Authors: Greenberg, R, Groves, M L, Dower, H J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Carboxypeptidase B
Carboxypeptidases
Carboxypeptidases A
Caseins - isolation & purification
Cattle
Cyanogen Bromide
Fundamental and applied biological sciences. Psychology
Holoproteins
Humans
Other proteins
Peptide Fragments - analysis
Phosphopeptides - analysis
Phosphorylation
Proteins
Sheep
Species Specificity
Trypsin
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Summary:The primary structure of human beta-casein has been determined by automated Edman degradation of the intact protein and of peptides derived therefrom by hydrolysis with trypsin and by chemical cleavage with cyanogen bromide. For each form of this multiphosphorylated protein (0-5 P/molecule), phosphorylated sites at specific seryl and threonyl residues have been identified. These are located near the amino terminus, within the first 10 residues of this 212-amino acid molecule. Sequence comparison of human beta-casein with the bovine and ovine proteins reveals 50% identity and a 10-residue shifted alignment relationship. Locations of prolyl and charged residues are generally conserved for the three homologues. The sequence data indicate the existence of genetic polymorphism involving uncharged residues in human beta-casein.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)42966-8