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[大鼠恶性肉瘤-45肌球蛋白的纯化及生化特性]

[Purification and biochemical characteristics of myosin from rat malignant sarcoma-45].

作者信息

Senchuk V V, Pikulev A T, Sholukh M V

出版信息

Biokhimiia. 1989 Dec;54(12):1939-46.

PMID:2534471
Abstract

Myosin was purified from rat tumour sarcoma-45 whose properties (effects of cations on ATPase activity, substrate specificity, temperature- and pH-optima, thermal stability, sensitivity of Mg2(+)-ATPase to F-actin, molecular mass, subunit composition) are similar to those of fast skeletal muscle myosin. Some parameters of the protein, namely, the levels of Ca2(+)- and K+, EDTA-ATPase activity, relative content of myosin light chains with Mr 16500 and the degree of tumoural myosin Mg2(+)-ATPase activation by F-actin, were significantly lower than those of skeletal muscle myosin.

摘要

肌球蛋白是从大鼠肿瘤肉瘤-45中纯化得到的,其特性(阳离子对ATP酶活性的影响、底物特异性、温度和pH最佳值、热稳定性、Mg2(+)-ATP酶对F-肌动蛋白的敏感性、分子量、亚基组成)与快收缩骨骼肌肌球蛋白相似。该蛋白质的一些参数,即Ca2(+)-和K+、EDTA-ATP酶活性水平、Mr 16500的肌球蛋白轻链相对含量以及F-肌动蛋白对肿瘤肌球蛋白Mg2(+)-ATP酶的激活程度,均显著低于骨骼肌肌球蛋白。

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