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  • Title: Complete primary structure of protein phosphatase inhibitor-1 from rabbit skeletal muscle.
    Author: Aitken A, Bilham T, Cohen P.
    Journal: Eur J Biochem; 1982 Aug; 126(2):235-46. PubMed ID: 6290217.
    Abstract:
    The complete primary structure of protein phosphatase inhibitor-1 has been determined. The protein consists of a single polypeptide chain of 165 residues, molecular weight 18640. The threonine residue that must be phosphorylated for activation is at position 35 and the active cyanogen bromide peptide, CB-1, comprises residues 2-66. The N-terminal methionine is acetylated and 40% of the inhibitor-1 molecules lack the C-terminal dipeptide Ala-Val. Serine-67 is substantially phosphorylated in vivo, but this phosphoserine residue does not appear to influence the activity of inhibitor-1.
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