Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack

Yoshie Satoh, Misako Nakaya, Yoshihiro Ochiai, Shugo Watabe

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25 Citations (Scopus)


Enzymatic and structural properties of white croaker fast skeletal muscle myosin were determined and compared with those of walleye pollack counterpart. Ca2+-ATPase activity of white croaker myosin was decreased to approximately 70% of the original activity during 1 day of storage at 0°C and pH 7.0 in 0.5 M KCl and 0.1 mM dithiothreitol, whereas that of walleye pollack was decreased to approximately 20% under the same condition. The activation energy (Ea) for inactivation of white croaker myosin calculated by the Arrhenius plot for inactivation rate constant (KD) was 1.2-fold higher than that of walleye pollack. While Ca2+-ATPase showed a similar KCl-dependency for the two species, the maximal activity was observed at pH 6.2 and 6.3 for white croaker and walleye pollack, respectively. Actin-activated myosin Mg2+-ATPase activity of white croaker was approximately half that of walleye pollack at 0.05 M KCl and pH 7.0, although the two myosins showed a similar affinity to F-actin with Km of 1.7 and 1.4, respectively. Limited proteolysis with α-chymotrypsin cleaved heat-denatured white croaker myosin mainly at heavy meromyosin/light meromyosin (HMM/LMM) junction, whereas walleye pollack myosin was cleaved at several sites in LMM as well as at the HMM/LMM junction.

Original languageEnglish
Pages (from-to)646-655
Number of pages10
JournalFisheries Science
Issue number3
Publication statusPublished - 2006 Jun
Externally publishedYes


  • ATPase
  • Actin activation
  • Fast skeletal muscle
  • Myosin
  • Proteolysis
  • Stability
  • Walleye pollack
  • White croaker

ASJC Scopus subject areas

  • Aquatic Science


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