借助偏振紫外荧光显微镜对收缩性肌肉蛋白结构变化的研究。1. ATP及其类似物引起的肌纤维中F-肌动蛋白的构象变化

[Study of structural changes of contractile muscle proteins with the aid of polarization ultraviolet fluorescence microscopy. 1. Conformational changes of F-actin in the muscle fiber caused by ATP and its analogs].

作者信息

Borovikov Iu S, Chernogriadskaia N A, Bogdanova M S, Rozanov Iu M, Kirillina V P

出版信息

Tsitologiia. 1976 Nov;18(11):1371-7.

Abstract

Increase of anisotropy of F-actin fluorescence of balanus and rabbit muscle fibers under the influence of ATP, AMP and pyrophosphate in EGTA presence was detected by means of the polarized ultraviolet (UV) fluorescent microscopy methods. The fluorescence anisotropy changes are assumed to be associated with the conformational changes in the actin. ATP cause more noticeable changes of actin structure, than pyrophosphate and AMP. The conformational changes in the actin of balanus and rabbit muscle fibres were similar. ATP and its analogs induced also decrease of UV fluorescence anisotropy of A-band which appears to be associated with conformational changes in myosin. It was siggested that the changes in fluorescence of anisotropy of A-bands are due to structural changes in both HMM and LMM parts of myosin molecule.

摘要

在存在乙二醇双（2-氨基乙基醚）四乙酸（EGTA）的情况下，通过偏振紫外（UV）荧光显微镜方法检测了ATP、AMP和焦磷酸对藤壶和兔肌肉纤维F-肌动蛋白荧光各向异性的影响。荧光各向异性的变化被认为与肌动蛋白的构象变化有关。与焦磷酸和AMP相比，ATP引起的肌动蛋白结构变化更明显。藤壶和兔肌肉纤维肌动蛋白的构象变化相似。ATP及其类似物还诱导了A带UV荧光各向异性的降低，这似乎与肌球蛋白的构象变化有关。有人认为，A带荧光各向异性的变化是由于肌球蛋白分子的重酶解肌球蛋白（HMM）和轻酶解肌球蛋白（LMM）部分的结构变化所致。

相似文献

1

[Study of structural changes of contractile muscle proteins with the aid of polarization ultraviolet fluorescence microscopy. 1. Conformational changes of F-actin in the muscle fiber caused by ATP and its analogs].

Tsitologiia. 1976 Nov;18(11):1371-7.

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