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. 1982 Aug 15;206(2):319–328. doi: 10.1042/bj2060319

Non-correlation of phosphorylation of the P-light chain and the actin activation of the ATPase of chicken gizzard myosin.

H A Cole, R J Grand, S V Perry
PMCID: PMC1158588  PMID: 6128971

Abstract

1. The enzymic properties of myosin isolated from chicken gizzard by three different methods have been compared. 2. Although the specific Ca2+-stimulated ATPases of all preparations were similar and high, there were significant differences in the specific activities of the Mg2+-stimulated actomyosin ATPases. 3. There was no direct correlation between the Mg2+-stimulated actomyosin ATPase activity and the extent of P-light-chain phosphorylation in any of the three myosin preparations. 4. A fraction that activates the Mg2+-stimulated actomyosin ATPase of gizzard muscle has been isolated from a gizzard muscle filament preparation. 5. The activator was specific for the Mg2+-activated actomyosin ATPase of smooth muscle. 6. The activator required the addition of calmodulin for full effect.

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Selected References

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