このエントリーをはてなブックマークに追加
ID 25988
file
title alternative
TWO-DIMENSIONAL ELECTROPHORETIC ANALYSIS OF MYOPROTEINS IN DEVELOPING RAT SKELETAL MUSCLE
creator
Miyahara, Hideaki
Katsuta, Shigeru
subject
two-dimensional gel electrophoresis
myoprotein
myosin light chain
isozyme
tropomyosin
NDC
Medical sciences
abstract
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.
journal title
体力科学 : Japanese Journal of Physical Fitness and Sports Medicine
volume
Volume 37
issue
Issue 2
start page
172
end page
182
date of issued
1988-04-01
publisher
日本体力医学会
issn
0039-906X
ncid
language
jpn
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
publisher
rights
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
relation url
department
Graduate School of Integrated Arts and Sciences