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   <subfield code="a">Lower Activation Energy for Sliding of F-Actin on a Less Thermostable Isoform of Carp Myosin</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Shigeru Chaen, Misako Nakaya, Xiao-Feng Guo, Shugo Watabe]</subfield>
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   <subfield code="a">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.</subfield>
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   <subfield code="a">© 1996 BY THE JOURNAL OF BIOCHEMISTRY</subfield>
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   <subfield code="a">in vitro motility assay</subfield>
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   <subfield code="t">The Journal of Biochemistry</subfield>
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