金属激活酶动力学研究方法。 - Suppr

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Approaches to kinetic studies on metal-activated enzymes.

作者信息

Morrison J F

出版信息

Methods Enzymol. 1979;63:257-94. doi: 10.1016/0076-6879(79)63013-6.

DOI:10.1016/0076-6879(79)63013-6

PMID:228154

Abstract

摘要

相似文献

Approaches to kinetic studies on metal-activated enzymes.金属激活酶动力学研究方法。

Methods Enzymol. 1979;63:257-94. doi: 10.1016/0076-6879(79)63013-6.

Studies on adenosine triphosphate transphosphorylases. XIII. Kinetic properties of the crystalline rabbit muscle ATP-AMP transphorphorylase (adenylate kinase) and a comparison with the crystalline calf muscle and liver adenylate kinases.三磷酸腺苷转磷酸酶的研究。十三。结晶兔肌ATP-AMP转磷酸酶（腺苷酸激酶）的动力学性质以及与结晶小牛肌和肝腺苷酸激酶的比较。

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NMR studies of the MgATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzyme.腺苷酸激酶的MgATP结合位点及该酶一个45个残基的肽片段的核磁共振研究。

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Studies of adenosine triphosphate transphosphorylases. XIV. Equilibrium binding properties of the crystalline rabbit and calf muscle ATP--AMP transphosphorylase (adenylate kinase) and derived peptide fragments.三磷酸腺苷转磷酸酶的研究。十四。结晶兔肌和小牛肌ATP-AMP转磷酸酶（腺苷酸激酶）及其衍生肽片段的平衡结合特性。

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