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The effect of hydrostatic pressure on the interaction of actomyosin subfragment 1 with nucleotides.

作者信息

McKillop D F, Geeves M A, Balny C

机构信息

Department of Biochemistry, University of Bristol, U.K.

出版信息

Biochem Biophys Res Commun. 1991 Oct 31;180(2):552-7. doi: 10.1016/s0006-291x(05)81100-3.

DOI:10.1016/s0006-291x(05)81100-3
PMID:1835384
Abstract

Increased hydrostatic pressure has previously been shown to reduce the tension of isometrically contracting skinned muscle fibres. An isomerization of the actomyosin complex is known to be pressure sensitive, but the pressure sensitivity of other steps in the ATPase pathway has not been characterised. We report here the effect of pressure on the ATP hydrolysis step of the myosin subfragment 1 ATPase, ADP binding to actomyosin subfragment 1 and the rate of ATP induced dissociation of actomyosin subfragment 1. We discuss the relationship of these changes to the observed effect of pressure on skinned muscle fibres.

摘要

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引用本文的文献

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