FAST SKELETAL MYOSIN ISOFORMS IN THERMALLY ACCLIMATED CARP

被引：60

作者：

WATABE, S ^{[1
]}

HWANG, GC ^{[1
]}

NAKAYA, M ^{[1
]}

GUO, XF ^{[1
]}

OKAMOTO, Y ^{[1
]}

机构：

[1] MURORAN INST TECHNOL,DEPT APPL CHEM,MURORAN,HOKKAIDO 050,JAPAN

来源：

JOURNAL OF BIOCHEMISTRY | 1992年 / 111卷 / 01期

关键词：

D O I：

10.1093/oxfordjournals.jbchem.a123706

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fast skeletal myosins were isolated from carp acclimated to 10 and 30-degrees-C, and their structural and enzymatic properties were compared. Myosins in 0.5 M KCl were subjected to limited proteolysis by using various proteases including alpha-chymotrypsin, trypsin, and papain, and different SDS-PAGE patterns were seen for the 10- and 30-degrees-C-acclimated myosins in all cases. Myosin subfragment-1 (S1) prepared from the 10-degrees-C-acclimated myosin by alpha-chymotryptic digestion in 0.12 M NaCl showed higher acto-S1 Mg2+-ATPase activity and lower thermostability than S1 from the warm-acclimated myosin. The peptide maps and ATP-induced spectral changes of tryptophan fluorescence also showed an obvious difference between the two types of S1. Temperature acclimation further caused changes in the rod region of myosin, since the apparent sizes of light meromyosin were different from each other for the two types of myosin. Myosin from carp acclimated to 20-degrees-C showed intermediate properties between those of the 10- and 30-degrees-C-acclimated myosins. Myosin isoforms might be expressed in a temperature-dependent manner to compensate for the effect of seasonal environmental temperature variation on swimming ability.

引用

页码：113 / 122

页数：10

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