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. 1989 Feb;89(2):586–589. doi: 10.1104/pp.89.2.586

Actin and Myosin in Pea Tendrils 1

Yong-Ze Ma 1, Lung-Fei Yen 1
PMCID: PMC1055885  PMID: 16666586

Abstract

We demonstrate here the presence of actin and myosin in pea (Pisum sativum L.) tendrils. The molecular weight of tendril actin is 43,000, the same as rabbit skeletal muscle actin. The native molecular weight of tendril myosin is about 440,000. Tendril myosin is composed of two heavy chains of molecular weight approximately 165,000 and four (two pairs) light chains of 17,000 and 15,000. At high ionic strength, the ATPase activity of pea tendril myosin is activated by K+-EDTA and Ca2+ and is inhibited by Mg2+. At low ionic strength, the Mg2+-ATPase activity of pea tendril myosin is activated by rabbit skeletal muscle F-actin. Superprecipitation occurred after incubation at room temperature when ATP was added to the crude actomyosin extract. It is suggested that the interaction of actin and myosin may play a role in the coiling movement of pea tendril.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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