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[细胞能量支持酶与肌纤维细肌丝的F-肌动蛋白的相互作用。I. 乳酸脱氢酶与F-肌动蛋白的结合诱导复合物组分结构状态的变化]

[Interaction of the enzymes of cellular energy support with the F-actin of the thin filaments of muscle fiber. I. The binding of lactate dehydrogenase with F-actin induces changes in the structural state of the components of the complex].

作者信息

Kirillina V P, Stabrovskaia V I, Borovikov Iu S

出版信息

Tsitologiia. 1988 Jul;30(7):841-8.

PMID:2973167
Abstract

A study was made of changes in F-actin conformation occurring in a myosin-free single ghost fibre induced by the binding of glycolytic enzyme lactate dehydrogenase (LDG) to F-actin. The formation of the complex between LDG and F-actin induces changes in the parameters of the intrinsic (tryptophan) and extrinsic (rodominil--phalloin) polarized fluorescence of F-actin of the ghost muscle fibre. It is found that LDG stimulates Mg2+-ATPase of actomyosin in solution. It is assumed that the coupling of energy-providing mechanism with that of muscle contraction may be accomplished through the conformation changes in F-actin.

摘要

对在无肌球蛋白的单个鬼肌纤维中，因糖酵解酶乳酸脱氢酶（LDG）与F-肌动蛋白结合而发生的F-肌动蛋白构象变化进行了研究。LDG与F-肌动蛋白之间复合物的形成，会导致鬼肌纤维F-肌动蛋白的固有（色氨酸）和外在（罗达明-鬼笔环肽）偏振荧光参数发生变化。研究发现，LDG可刺激溶液中肌动球蛋白的Mg2 + -ATP酶。据推测，能量供应机制与肌肉收缩机制的耦合可能是通过F-肌动蛋白的构象变化来实现的。

相似文献

1
[Interaction of the enzymes of cellular energy support with the F-actin of the thin filaments of muscle fiber. I. The binding of lactate dehydrogenase with F-actin induces changes in the structural state of the components of the complex].[细胞能量支持酶与肌纤维细肌丝的F-肌动蛋白的相互作用。I. 乳酸脱氢酶与F-肌动蛋白的结合诱导复合物组分结构状态的变化]
Tsitologiia. 1988 Jul;30(7):841-8.
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Lactate dehydrogenase-induced conformational changes of F-actin in myosin-free ghost single fibres.乳酸脱氢酶诱导无肌球蛋白空壳单纤维中F-肌动蛋白的构象变化。
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