A myofibrillar protein phosphatase from rabbit skeletal muscle contains the β isoform of protein phosphatase‐1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosin

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Abstract
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. PP1M, which eluted from Superose 12 with an apparent molecular mass of 60 kDa, was dissociated by LiBr into two subunits. One of these displayed enzymic properties identical to those of the catalytic subunit of protein phosphatase‐1 (PP1C) and was identified as the β isoform of PP1C by amino acid sequencing. The second subunit had no intrinsic protein phosphatase activity, but greatly increased the rate at which PP1C dephosphorylated skeletal‐muscle heavy meromyosin and decreased the rate at which it dephosphorylated glycogen phosphorylase.The properties of PP1M, together with those of smooth muscle PP1M [Alessi, D., MacDougall, L. K., Sola, M. M., Ikebe, M. & Cohen, P. (1992) Eur. J. Biochem. 210, 1023–1035] and the previously characterised glycogen‐associated form of protein phosphatase‐1 (PP1G), indicate that the subcellular localisation and substrate specificity of PP1 is determined by its interaction with specific targetting subunits.