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猪心肌肌钙蛋白原的自旋标记研究。

A spin labeling study of pig cardiac tropomyosin.

作者信息

Ye H P, Wang H L, Sheng P G, Zou Y S

机构信息

Shanghai Institute of Biochemistry, Academia Sinica.

出版信息

Sci China B. 1989 Mar;32(3):324-34.

PMID:2551334
Abstract

Tropomyosin (TM) extracted from pig cardiac muscle was spin-labeled with 2,2,6,6-tetramethyl-4-(dichlorotriazin)-aminopiperidine-1-oxyl. The ESR spectra of the product (SL-TM) were of a type of weak immobilization. Effects of three means for the denaturation were observed on the above spectra. The ESR spectrum obtained for SL-TM after enzymatic degradation was found to be analogous to that for the label itself in a dilute solution and thereby the quantity of labels bound in SL-TM estimated. The Arrhenius plots attained through variable temperature measurement for SL-TM's exhibited two inflexion points (the conformational transition temperatures for TM) around 45 degrees C and 74-75 degrees C, the latter temperature having not been reported in literature so far. However, the enzymatic degradation product from SL-TM behaved quite differently from it in the response to microwave power saturation and temperature variation.

摘要

从猪心肌中提取的原肌球蛋白(TM)用2,2,6,6-四甲基-4-(二氯三嗪)-氨基哌啶-1-氧基进行自旋标记。产物(SL-TM)的电子自旋共振(ESR)谱属于弱固定化类型。观察了三种变性方法对上述谱图的影响。发现酶促降解后SL-TM的ESR谱与稀溶液中标记物本身的谱相似,从而估算出SL-TM中结合的标记物数量。通过对SL-TM进行变温测量得到的阿伦尼乌斯曲线在约45℃和74 - 75℃处出现两个拐点(TM的构象转变温度),后者温度迄今尚未见文献报道。然而,SL-TM的酶促降解产物在对微波功率饱和及温度变化的响应方面表现与它截然不同。

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