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Identification of functional differences between recombinant human ? and ? cardiac myosin motors

Deacon, John C., Bloemink, Marieke J., Rezavandi, Heresh, Geeves, Michael A., Leinwand, Leslie A. (2012) Identification of functional differences between recombinant human ? and ? cardiac myosin motors. Cellular and Molecular Life Sciences, 69 (13). pp. 2261-2277. ISSN 1420-682X. (doi:10.1007/s00018-012-0927-3)

Abstract

The myosin isoform composition of the heart is

contractile velocity and force generation. While different

b myosin heavy chain, healthy human heart ventricles

failing human ventricles express no detectable a-myosin.

a and b myosin heavy chain motor domains. This represents the ?rst such analysis of any human muscle myosin

?ndings reveal substantial isoform differences in individual

(S1) is far more similar to adult fast skeletal muscle myosin

identity between the motor domains of a- and b-myosin.

ATP hydrolysis step of a-S1 is *ten-fold faster than b-S1,

and actin a-S1 exhibits rapid ADP release, which is > tenfold faster than ADP release for b-S1. Overall, the cycle

each myosin spends tightly bound to actin (the duty ratio)

underlie the basis for this ?nding.

Item Type: Article
DOI/Identification number: 10.1007/s00018-012-0927-3
Uncontrolled keywords: Muscle, Kinetics, ATPase, Contraction, Heart
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 20 Jun 2012 14:28 UTC
Last Modified: 23 Jan 2020 04:05 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/29670 (The current URI for this page, for reference purposes)
Geeves, Michael A.: https://orcid.org/0000-0002-9364-8898
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