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[利用核磁共振磷谱法对肌球蛋白的Mg2+-ATP酶反应进行研究。在纯化的肌球蛋白亚片段I中检测腺苷酸激酶活性]

[Study of the Mg2+-ATPase reaction of myosin using the NMR-31P method. Detection of adenylate kinase activity in a purified myosin subfragment I].

作者信息

Levitskiĭ D I, Rusak A F, Kashtanova N L, Vorontsov E D, Ebdakov V P

出版信息

Biokhimiia. 1979 Sep;44(9):1721-4.

PMID:228775
Abstract

Isolated myosin heads (HMM-S1) were concentrated by ultrafiltration in an "Amicon" cell to a concentration of 120 mg/ml. Incubation of HMM-S1 with ATP in the presence of Mg2+ produced an AMP peak in the spectrum of NMR-31P whose size was increasing linearly with the reaction time. It was demonstrated that after heating of the sample the appearance of AMP in the incubation mixture was due to the presence of a small amount of adenylate kinase (or myokinase) in the purified preparation of HMM-S1.

摘要

通过在“Amicon”细胞中进行超滤,将分离出的肌球蛋白头部(HMM-S1)浓缩至浓度为120 mg/ml。在Mg2+存在的情况下,HMM-S1与ATP孵育,在NMR-31P光谱中产生一个AMP峰,其大小随反应时间呈线性增加。结果表明,样品加热后,孵育混合物中AMP的出现是由于纯化的HMM-S1制剂中存在少量腺苷酸激酶(或肌激酶)。

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