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1993/06/30
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Calponin phosphatase from smooth muscle : A possible role of type 1 protein phosphatase in smooth muscle relaxation.

Ichikawa K, Ito M, Okubo S, Konishi T, Nakano T, Mino T, Nakamura F, Naka M, Tanaka T.
Biochem Biophys Res Commun. 1993 Jun 30;193(3):827-33.

Abstract

Smooth muscle myosin bound phosphatase (MBP) purified from chicken gizzard, which is a holoenzyme of type 1 delta protein phosphatase and dephosphorylated intact myosin, catalyzed the dephosphorylation of calponin phosphorylated by protein kinase C (PK-C). The Km of MBP for calponin was 0.6 microM and the Vmax was 350 nmol/min/mg. All of the multiple sites of phosphorylation by PK-C of calponin were completely dephosphorylated by MBP. Functionally, calponin dephosphorylated by MBP recovered its inhibitory effect on the actin-activated Mg(2+)-ATPase activity of myosin. Therefore, these results suggest that a type 1 delta protein phosphatase causes relaxation of smooth muscle by the dephosphorylation not only of myosin but also of calponin.

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