Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle.
作者： A Shirazi , K Iizuka , P Fadden , C Mosse , A P Somlyo
DOI: 10.1016/S0021-9258(18)31736-8
关键词: Biology 、 Protein subunit 、 Myosin phosphatase activity 、 Myosin-light-chain phosphatase 、 Heterotrimeric G protein 、 Myofibril 、 Myosin light-chain kinase 、 Dephosphorylation 、 Myosin 、 Biochemistry
摘要: We have purified to homogeneity from the myofibrillar fraction of pig bladder a mammalian heterotrimeric form PP-1, SMPP-1M. Purified SMPP-1M is similar in composition and substrate specificity avian gizzard PP-1M reported by Alessi et al. (Alessi, D., Macdougall, L. K., Sola, M. M., Ikebe, Cohen, P. (1992) Eur. J. Biochem. 210, 1023-1035) consists catalytic subunit PP-1 (37 kDa) two other equimolar subunits 130 20 kDa. The properties role its regulatory dephosphorylation myosin initiation relaxation were characterized both vitro smooth muscle. show that relaxant effect muscle markedly potentiated addition Our findings demonstrate major phosphatase dephosphorylating regulated vivo via targeting specifically alter PP-1C toward myosin.
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