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衰老大鼠骨骼肌肌球蛋白A和肌动球蛋白的酶学研究。

Enzymatic studies on the skeletal myosin A and actomyosin of aging rats.

作者信息

Kaldor G, Min B K

出版信息

Fed Proc. 1975 Feb;34(2):191-4.

PMID:123207
Abstract

Myosin A and actomyosin were isolated from the skeletal muscle of old and young rats. The velocity of the Ca2+ activated myosin A ATPase was increased in the case of the older animals. On the other hand the velocity of the Mg-2plus activated actomyosin ATPase was decreased in the skeletal muscle of the aging rats. At 5 X 10-5M EGTA concentration the inhibition of the Mg-2plus activated myosin B ATPase of the 1-month-old rats was two- to threefold smaller than that of the older animals. It was shown that the myosin A component of the actomyosin was responsible for the decreased troponin inhibition in the case of the 1-month-old rats. Between the ages of 1 month and 29 months the number of free myosin A SH groups decreases by 50%. The lipid peroxidation in the muscle of the 1-month-old animals.

摘要

从老年和幼年大鼠的骨骼肌中分离出肌球蛋白A和肌动球蛋白。老年动物中,Ca2+激活的肌球蛋白A ATP酶的速度增加。另一方面,衰老大鼠骨骼肌中Mg2+激活的肌动球蛋白ATP酶的速度降低。在5×10-5M EGTA浓度下,1月龄大鼠的Mg2+激活的肌球蛋白B ATP酶的抑制作用比老年动物小两到三倍。结果表明,1月龄大鼠的肌动球蛋白中的肌球蛋白A成分是肌钙蛋白抑制作用降低的原因。在1个月至29个月龄之间,游离肌球蛋白A SH基团的数量减少了50%。1月龄动物肌肉中的脂质过氧化。

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