caa a22 4500 46582658X CHVBK 20180323112151.0 cr unu---uuuuu 170327e19900801xx s 000 0 eng 10.1007/BF00302588 doi (NATIONALLICENCE)springer-10.1007/BF00302588 Changes in carp myosin ATPase induced by temperature acclimation [Elektronische Daten] [G. Hwang, S. Watabe, K. Hashimoto] Summary: Myosins were isolated from dorsal ordinary muscles of carp acclimated to 10°C and 30°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 measured at pH 7.0. The highest activity was 0.32 μmol Pi·min-1·mg-1 at 0.2 M KCl for cold-acclimated carp and 0.47 μmol Pi·min-1·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 μmol Pi·min-1·mg-1 at pH 6 and 0.4 μmol Pi·min-1·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 μmol Pi·min-1·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 μmol Pi·min-1·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 25·10-4·s-1 at 30°C and pH 7.0 for 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. Springer-Verlag, 1990 Temperature nationallicence Acclimation nationallicence Myosin nationallicence Myosin heavy chain nationallicence ATPase activity nationallicence Carp nationallicence ATPase : adenosine 5′-triphosphatase nationallicence DTNB 5,5′ : dithio-bis-2-nitrobenzoic acid nationallicence DTT : dithiothreitol nationallicence EGTA : ethyleneglycol bis (β-aminoethylether)-N,N,N′,N′-tetraacetic acid nationallicence K D : inactivation rate constant nationallicence SDS : sodium dodecyl sulfate nationallicence SDS-PAGE : SDS-polyacrylamide gel electrophoresis nationallicence Hwang G. Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, 113, Bunkyo, Tokyo, Japan aut Watabe S. Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, 113, Bunkyo, Tokyo, Japan aut Hashimoto K. Food Science Laboratory, Faculty of Education, Ibaraki University, 310, Mito, Ibaraki, Japan aut Journal of Comparative Physiology B Springer-Verlag 160/3(1990-08-01), 233-239 0174-1578 160:3<233 1990 160 360 https://doi.org/10.1007/BF00302588 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00302588 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hwang G. Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, 113, Bunkyo, Tokyo, Japan aut NATIONALLICENCE 700 1- Watabe S. Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, 113, Bunkyo, Tokyo, Japan aut NATIONALLICENCE 700 1- Hashimoto K. Food Science Laboratory, Faculty of Education, Ibaraki University, 310, Mito, Ibaraki, Japan aut NATIONALLICENCE 773 0- Journal of Comparative Physiology B Springer-Verlag 160/3(1990-08-01), 233-239 0174-1578 160:3<233 1990 160 360 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer