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A myofibrillar protein phosphatase from rabbit skeletal muscle contains the beta isoform of protein phosphatase-1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosin.
Dent P, MacDougall LK, MacKintosh C, Campbell DG, Cohen P. Dent P, et al. Among authors: cohen p. Eur J Biochem. 1992 Dec 15;210(3):1037-44. doi: 10.1111/j.1432-1033.1992.tb17509.x. Eur J Biochem. 1992. PMID: 1336456 Free article.
A form of protein phosphatase-1 (PP1M), which possesses 25-fold higher activity towards the P light chain of myosin (in heavy meromyosin) than other forms of protein phosphatase-1, was purified over 200,000-fold from the myofibrillar fraction of rabbit skeletal muscle. ... …
A form of protein phosphatase-1 (PP1M), which possesses 25-fold higher activity towards the P light chain of myosin (in heavy meromyo …
4,300 results