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. 1989 Feb;89(2):586-9.
doi: 10.1104/pp.89.2.586.

Actin and Myosin in pea tendrils

Y Z Ma  1 , L F Yen
Affiliations

Actin and Myosin in pea tendrils

Y Z Ma et al. Plant Physiol. 1989 Feb.

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 Ca(2+) and is inhibited by Mg(2+). At low ionic strength, the Mg(2+)-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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References

    1. Exp Cell Res. 1974 Oct;88(2):435-9 - PubMed
    1. J Biochem. 1979 Feb;85(2):375-8 - PubMed
    1. Arch Biochem Biophys. 1972 Jan;148(1):199-297 - PubMed
    1. J Biochem. 1977 Sep;82(3):777-82 - PubMed
    1. Plant Physiol. 1966 Sep;41(7):1152-8 - PubMed

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