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

被引:31
作者
Satoh, Yoshie [1 ]
Nakaya, Misako [1 ]
Ochiai, Yoshihiro [1 ]
Watabe, Shugo [1 ]
机构
[1] Univ Tokyo, Lab Aquat Mol Biol & Biotechnol, Grad Sch Agr & Life Sci, Bunkyo Ku, Tokyo 1138657, Japan
关键词
actin activation; ATPase; fast skeletal muscle; myosin; proteolysis; stability; walleye pollack; white croaker;
D O I
10.1111/j.1444-2906.2006.01195.x
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
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 degrees 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 (E-a) for inactivation of white croaker myosin calculated by the Arrhenius plot for inactivation rate constant (K-D) 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 K-m of 1.7 and 1.4, respectively. Limited proteolysis with alpha-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.
引用
收藏
页码:646 / 655
页数:10
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