Aitken A, Bilham T, Cohen P
Eur J Biochem. 1982 Aug;126(2):235-46. doi: 10.1111/j.1432-1033.1982.tb06771.x.
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.
已确定蛋白磷酸酶抑制剂-1的完整一级结构。该蛋白由一条含165个残基的单多肽链组成，分子量为18640。激活所需磷酸化的苏氨酸残基位于第35位，活性溴化氰肽CB-1包含第2至66位残基。N端甲硫氨酸被乙酰化，40%的抑制剂-1分子缺少C端二肽丙氨酸-缬氨酸。丝氨酸-67在体内大量磷酸化，但该磷酸丝氨酸残基似乎不影响抑制剂-1的活性。
