Purification of Gizzard Myosin Light-Chain Phosphatase, and Reversible Changes in the ATPase and Superprecipitation Activities of Actomyosin in the Presence of Purified Preparations of Myosin Light-Chain Phosphatase and Kinase1

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Population

Gizzard myosin light-chain phosphatase (MLCP) and kinase (MLCK) preparations and actomyosin suspensions

Design

Preclinical

Authors

Discussion

Provides mechanistic insight into Ca2+-dependent smooth muscle regulation via MLCK/MLCP; leaves open translation to mammalian cardiovascular models.

Population

Gizzard myosin light-chain phosphatase (MLCP) and kinase (MLCK) preparations and actomyosin suspensions

Intervention

Addition of purified MLCP and MLCK, and Ca2+

Outcome

Reversible changes in ATPase and superprecipitation activities, and turbidity of actomyosin suspensionssurrogate

Purified MLCP and MLCK play a key role in Ca2+ regulation of actomyosin in gizzard smooth muscle.

Onishi et al. (1982) studied this question.

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Provides mechanistic insight into Ca2+-dependent smooth muscle regulation via MLCK/MLCP; leaves open translation to mammalian cardiovascular models.