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原肌球蛋白中保守的功能特性。

The functional characteristics conserved in tropomyosins.

作者信息

Hayashi J, Hirabayashi T

出版信息

J Biochem. 1978 Feb;83(2):341-8. doi: 10.1093/oxfordjournals.jbchem.a131919.

Abstract
  1. Tropomyosin, one of the regulatory proteins in muscle contraction, was prepared from chickens, rabbits, frogs, shrimps, and shellfish, and conserved characteristics were studied using an enzymological technique. 2. All tropomyosins tested, irrespective of their sources, were found to have the ability to mediate the inhibitory activity of rabbit troponin toward rabbit Mg2+-activated actomyosin ATPase (Mg2+-ATPase) activity in the absence of Ca2+ ions. 3. The effect of tropomyosin on the Mg2+-ATPase activity in the presence of Ca2+ ions varied, depending on the source, and this variation appeared to reflect the evolutionary course of this protein. 4. Tropomyosin from shellfish adductor muscle had the ability to bind to rabbit skeletal muscle troponin and actin. This ability is also considered to be a basic characteristic of tropomyosin which has been conserved during evolution.
摘要
  1. 原肌球蛋白是肌肉收缩中的调节蛋白之一,从鸡、兔、蛙、虾和贝类中提取,并采用酶学技术研究其保守特性。2. 所有测试的原肌球蛋白,无论其来源如何,在不存在钙离子的情况下,都被发现有能力介导兔肌钙蛋白对兔镁离子激活的肌动球蛋白ATP酶(Mg2+-ATP酶)活性的抑制作用。3. 在存在钙离子的情况下,原肌球蛋白对Mg2+-ATP酶活性的影响因来源而异,这种差异似乎反映了该蛋白质的进化过程。4. 贝类闭壳肌中的原肌球蛋白有能力与兔骨骼肌肌钙蛋白和肌动蛋白结合。这种能力也被认为是原肌球蛋白在进化过程中保守的基本特性。

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