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Title
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Human beta-casein. Amino acid sequence and identification of phosphorylation sites.
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Authors
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R.Greenberg,
M.L.Groves,
H.J.Dower.
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Ref.
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J Biol Chem, 1984,
259,
5132-5138.
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PubMed id
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Abstract
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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.
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