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大鼠和犬心肌α-辅肌动蛋白的物理化学性质

Physico-chemical properties of rat and dog cardiac alpha-actinin.

作者信息

Malhotra A, Margossian S S, Slayter H S

出版信息

Biochim Biophys Acta. 1986 Dec 12;874(3):347-54. doi: 10.1016/0167-4838(86)90034-8.

Abstract

alpha-Actinin exists in several polymorphic forms which appear to be characteristic of the muscle type from which it is isolated. In order to determine the possible physiological role of this structural protein in cardiac muscle, we describe and compare here the physico-chemical properties of cardiac alpha-actinin from two different mammalian species, rat (fast contracting muscle) and dog (slow contracting muscle). Purification of cardiac alpha-actinin was achieved by chromatography on DEAE-cellulose and hydroxyapatite columns. The alpha-actinins isolated were different in their electrophoretic mobility (SDS-polyacrylamide gel electrophoresis), molecular size and alpha-helical content. However, their shape as revealed by electron microscopy and their activating effect on Mg2+-ATPase activity of actomyosin appear to be similar. These studies suggest that the rat and dog cardiac alpha-actinin are structurally different but functionally similar proteins.

摘要

α-辅肌动蛋白以几种多态形式存在,这些形式似乎是其分离来源的肌肉类型所特有的。为了确定这种结构蛋白在心肌中的可能生理作用,我们在此描述并比较来自两种不同哺乳动物物种(大鼠,快速收缩肌肉;狗,慢速收缩肌肉)的心肌α-辅肌动蛋白的物理化学性质。通过在DEAE-纤维素柱和羟基磷灰石柱上进行色谱分离实现了心肌α-辅肌动蛋白的纯化。分离出的α-辅肌动蛋白在电泳迁移率(SDS-聚丙烯酰胺凝胶电泳)、分子大小和α-螺旋含量方面存在差异。然而,它们通过电子显微镜显示的形状以及对肌动球蛋白Mg2 + -ATP酶活性的激活作用似乎相似。这些研究表明,大鼠和狗的心肌α-辅肌动蛋白是结构不同但功能相似的蛋白质。

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