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PubMed · 186030

Myosin light-chain phosphatase.

M Morgan·S V Perry·J Ottaway
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Abstract

1. A method for the isolation of a new enzyme, myosin light-chain phosphatase, from rabbit white skeletal muscle by using a Sepharose-phosphorylated myosin light-chain affinity column is described. 2. The enzyme migrated as a single component on electrophoresis in sodium dodecyl sulphate/polyacrylamide gel at pH7.0, with apparent mol.wt. 70000. 3. The enzyme was highly specific for the phosphorylated P-light chain of myosin, had pH optima at 6.5 and 8.0 and was not inhibited by NaF. 4. A Ca2+-sensitive 'ATPase' (adenosine triphosphatase) system consisting of myosin light-chain kinase, myosin light-chain phosphatase and the P-light chain is described. 5. Evidence is presented for a phosphoryl exchange between Pi, phosphorylated P-light chain and myosin light-chain phosphatase. 6. Heavy meromyosin prepared by chymotryptic digestion can be phosphorylated by myosin light-chain kinase. 7. The ATPase activities of myosin and heavy meromyosin, in the presence and absence of F-actin, were not significantly changed (+/- 10%) by phosphorylation of the P-light chain.

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ActinsActomyosinAnimalsMagnesiumMolecular WeightMusclesMyosin SubfragmentsMyosinsPhosphatesPhosphoproteinsPhosphoric Monoester HydrolasesProtein KinasesRabbitsJournal Article

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M Morgan, S V Perry, J Ottaway. 1976-09-01. Myosin light-chain phosphatase.. https://doi.org/10.1042/bj1570687

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