Journal Article

Lower Activation Energy for Sliding of F-Actin on a Less Thermostable Isoform of Carp Myosin

Shigeru Chaen, Misako Nakaya, Xiao-Feng Guo and Shugo Watabe

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 120, issue 4, pages 788-791
Published in print October 1996 | ISSN: 0021-924X
Published online October 1996 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021480
Lower Activation Energy for Sliding of F-Actin on a Less Thermostable Isoform of Carp Myosin

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We have examined the temperature-dependence of sliding velocity of fluorescent F-actin on myosins isolated from 10°C- and 30°C-acclimated carp. Activation energies for the sliding of F-actin were 63 and 111 kJ/mol for the 10°C- and 30°C-acclimated carp myosins, respectively. Arrhenius plots of the sliding velocity from 10°C- and 30°C-acclimated carp myosin were shown to intersect at high temperature (about 30°C). The thermostability estimated by measuring the Ca2+-ATPase activity was less for myosin from 10°C- than 30°C-acclimated carp. We suggest that a less thermostable structure in cold-acclimated carp myosin results in a reduced activation energy for the contractile process, which allows the F-actin to slide fast even at low temperatures.

Keywords: activation energy; carp myosin; in vitro motility assay; temperature acclimation; thermostability

Journal Article.  0 words. 

Subjects: Biochemistry

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