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[通过自旋标记蛋白的饱和电子顺磁共振光谱研究底物和顺磁性锰离子与磷酸甘油酸激酶的结合]

[Study of the binding of substrates and paramagnetic Mn2+ ions with phosphoglycerate kinase by saturating ESR spectra of a spin-labelled protein].

作者信息

Vlasova I I, Kuprin S P

出版信息

Biofizika. 1992 Sep-Oct;37(5):910-9.

PMID:1335290
Abstract

A single SH-group of phosphoglycerate kinase from yeast was modified by mercury-containing spin label. The saturation curves of ESR spectra of the spin-labeled enzyme were studied. The paramagnetic ions of Mn2+ bound to the centre of ion nonspecific binding or active centre in the complex with ATP can influence the saturation of the spin-labeled enzyme. The saturation curves of the ESR signal of the spin-labeled enzyme in the presence of paramagnetic complex of CrATP were studied. It has been demonstrated that the second nonspecific centre of ATP binding is located at the active site of the enzyme (3-phosphoglycerate binding centre).

摘要

来自酵母的磷酸甘油酸激酶的单个巯基被含汞自旋标记修饰。研究了自旋标记酶的电子自旋共振(ESR)光谱的饱和曲线。与ATP形成复合物时,结合到离子非特异性结合中心或活性中心的Mn2+顺磁性离子可影响自旋标记酶的饱和。研究了在CrATP顺磁性复合物存在下自旋标记酶的ESR信号的饱和曲线。已证明ATP结合的第二个非特异性中心位于酶的活性位点(3-磷酸甘油酸结合中心)。

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