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ID 25988
本文ファイル
別タイトル
TWO-DIMENSIONAL ELECTROPHORETIC ANALYSIS OF MYOPROTEINS IN DEVELOPING RAT SKELETAL MUSCLE
著者
宮原 英昭
勝田 茂
キーワード
two-dimensional gel electrophoresis
myoprotein
myosin light chain
isozyme
tropomyosin
NDC
医学
抄録(英)
Changes in myoproteins during development of rat skeletal muscle were investigated using two-dimensional gel electrophoresis. In M. soleus (SOL) which in adult, is composed predolninantly of slow twitch fibers, fast type myosin light chains(fLC)were the major species and slow type light chains (sLC) were the minor species at birth. During development, the replacement rate of fLC to SLC sequentially occurred so that LC patterns at 21 days postpartum were similar to adult where fLC were difficult to visualize. In contrast, M. extensor digitorum . longus (EDL) always contained dominant fLC although SLC were found only for 5~ 9 days. LC 3 f became detectable at 5 days and gradually increased. In α-tropomyosin there were isozymes of fast and slow type based on difference in molecular weight, but not in β-tropomyosin. Changes in isozymes of α-tropomyosin approxhuately corresponded with that in isozymes (fast and slow type) of LC in both EDL and SOL. During adult stage following birth, in EDL creatine kinase underwent a three-fold increase in molecular ratio to actin, whereas in SOL there was little change though increase took place transiently. These results suggest that with development many myoproteins change more dramatically in slow muscle than in fast muscle, and that transitions in LC isozymes and changes in distribution of histochemically typed muscle fibers may follow different time courses.
掲載誌名
体力科学 : Japanese Journal of Physical Fitness and Sports Medicine
37巻
2号
開始ページ
172
終了ページ
182
出版年月日
1988-04-01
出版者
日本体力医学会
ISSN
0039-906X
NCID
言語
日本語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
publisher
権利情報
日本体力医学会
本文データは学協会の許諾に基づきCiNiiから複製したものである
関連情報URL
部局名
総合科学研究科