TROPOMYOSIN FROM THE STRIATED MUSCLES OF CARP (CYPRINUS-CARPIO) AND OF ICEFISH (CHANNICHTHYS-RHINOCERATUS)

被引:2
作者
FELLER, G [1 ]
DHAESE, J [1 ]
GERDAY, C [1 ]
机构
[1] UNIV DUSSELDORF,INST ZOOL,W-4000 DUSSELDORF 1,GERMANY
来源
ARCHIVES INTERNATIONALES DE PHYSIOLOGIE DE BIOCHIMIE ET DE BIOPHYSIQUE | 1990年 / 98卷 / 05期
关键词
D O I
10.3109/13813459009113990
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
Tropomyosin of fast-twitch, slow-twitch and cardiac muscles of carp and icefish has been isolated by hydroxyapatite chromatography. The subunit distribution has been investigated by polyacrylamide gel electrophoresis and by peptide mapping. The purified skeletal muscle tropomyosins all belong to the alpha-family and differ from higher vertebrate tropomyosin by the lack of beta-subunits. Specific alpha-isotypes are however encountered in fast-twitch fibres (alpha-w subunit) and slow-twitch or intermediate (pink) fibres (alpha and alpha-w subunits). The amino acid compositions and paracrystals formed by the carp alpha-w-alpha-w and alpha-alpha-w tropomyosins do not differ markedly from that of rabbit alpha-alpha-chains. They differ however by their capability to inhibit the ATPase activity of rabbit skeletal muscle acto-HMM system. A beta-like subunit is found in carp cardiac tropomyosin, in the proportion of 25% of the native protein, but not in icefish heart.
引用
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页码:297 / 305
页数:9
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