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Changes in carp myosin atpase induced by temperature acclimation



Changes in carp myosin atpase induced by temperature acclimation



Journal of Comparative Physiology B Biochemical Systemic & Environmental Physiology 160(3): 233-240



Myosins were isolated from dorsal ordinary muscles of carp acclimated to 10.degree.C and 30.degree.C for a minimum of 5 weeks and examined for their ATPase activities. Ca2+-ATPase activity was different between myosins from cold- and warm-acclimated carp, especially at KCl concentrations ranging from 0.1 to 0.2 M, when meausred at pH 7.0. The highest activity was 0.32 .mu.mol Pi .cntdot. min-1 .cntdot. mg-1 at 0.2 M KCl for cold-acclimated carp and 0.47 .mu.mol Pi .cntdot. min-1 .cntdot. mg-1 at 0.1 M KCl for warm-acclimated fish. The pH-dependency of Ca2+-ATPase activity at 0.5 M KCl for both carp was, however, similar exhibiting two maxima around 0.3 .mu.mol Pi .cntdot. min-1 .cntdot. mg-1 at pH 6 and 0.4 .mu.mol Pi .cntdot. min-1 .cntdot. mg-1 at pH 9. K+ (EDTA)-ATPase activity at pH 7.0 neither exhibited differences between both myosins. It increased with increasing KCl concentration showing the highest value of about 0.4 .mu.mol Pi .cntdot. min-1 .cntdot. mg-1 at 0.6-0.7 M KCl. Actin-activated myosin Mg2+-ATPase activity was markedly different between cold- and warm-acclimated carp. The maximum initial velocity was 0.53 .mu.mol Pi .cntdot. min-1 .cntdot. mg-1 myosin at pH 7.0 and 0.05 M KCl for cold-acclimated carp, which was 1.6 times as high as that for warm-acclimated carp. These differences were in good agreement with those obtained with myofibrillar Mg2+-ATPase activity between both carp. No differences were, however, observed in myosin affinity to actin. Differences in myosin properties between cold- and warm-acclimated carp were further evidenced by its thermal stability. The inactivation rate constant of myosin Ca2+-ATPase was 25 .cntdot. 10-4 .cntdot. s-1 at 30.degree.C and pH 7.0 fold cold-acclimated carp, which was about 4 times as high as that for warm-acclimated carp. Light chain composition did not differ between both carp myosins. The differences in a primary structure of the heavy chain subunit was, however, clearly demonstrated between both myosins by peptide mapping.

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Accession: 007091670

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DOI: 10.1007/bf00302588


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