Eto M, Ohmori T, Suzuki M, Furuya K, Morita F
Division of Chemistry, Hokkaido University.
J Biochem. 1995 Dec;118(6):1104-7. doi: 10.1093/oxfordjournals.jbchem.a124993.
A novel phosphorylation-dependent inhibitory protein (IP) of porcine aorta myosin light chain phosphatase (PA-MLCP) was purified to homogeneity from porcine aorta media. The molecular mass of IP was 20 kDa. IP phosphorylated by endogenous potentiating kinase (IP-K) inhibited not only PA-MLCP activity, but also that of the catalytic subunit of protein phosphatase-1. The amino acid sequence of a peptide derived from IP phosphorylated with IP-K, RHARVTVK, shared one of the consensus sequences phosphorylatable by protein kinase C (PKC), where T was phosphorylated. IP was phosphorylated by PKC and the phosphorylated product inhibited PA-MLCP as strongly as IP phosphorylated with IP-K.
一种新型的猪主动脉肌球蛋白轻链磷酸酶（PA-MLCP）的磷酸化依赖性抑制蛋白（IP）从猪主动脉中膜纯化至同质。IP的分子量为20 kDa。由内源性增强激酶（IP-K）磷酸化的IP不仅抑制PA-MLCP活性，还抑制蛋白磷酸酶-1催化亚基的活性。用IP-K磷酸化的IP衍生的肽RHARVTVK的氨基酸序列与蛋白激酶C（PKC）可磷酸化的共有序列之一相同，其中T被磷酸化。IP被PKC磷酸化，磷酸化产物对PA-MLCP的抑制作用与用IP-K磷酸化的IP一样强。
