Chemical modification as an approach to elucidation of sodium pump structure-function relations.

Chemical modification as an approach to elucidation of sodium pump structure-function relations.
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化学修饰作为阐明钠泵结构-功能关系的一种方法。

DOI:
10.1152/ajpcell.1990.258.1.c1
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发表时间:
1990
期刊:
The American journal of physiology
影响因子:
--
通讯作者:
Kaplan,JH
Kaplan,JH
中科院分区:
--
文献类型:
--
作者:
Pedemonte,CH;Kaplan,JH

文献摘要

被引文献

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对酶中特定残基进行化学修饰,并表征其抑制类型和修饰活性的性质,是蛋白质结构-功能研究中的一种既定方法。近年来,随着从基因克隆技术中获得初级序列信息的进展,这种策略变得更加富有成效。本文讨论了化学修饰方法在Na(+)-K(+)-ATP酶研究中的应用。由于抑制剂、配体、修饰剂和蛋白水解酶的联合使用,关于动力学、酶结构和各种构象状态的大量信息已经变得可用。我们将回顾各种试剂和方法,已被用来达到结构-功能相关性,并严格讨论从这些方法获得的信息类型的限制和模糊性。Na(+)泵蛋白的化学修饰已经提供了大量的数据,我们预计,当合适的表达系统变得可用时,将指导未来诱变研究的努力。
Chemical modification of specific residues in enzymes, with the characterization of the type of inhibition and properties of the modified activity, is an established approach in structure-function studies of proteins. This strategy has become more productive in recent years with the advances made in obtaining primary sequence information from gene-cloning technologies. This article discusses the application of chemical modification procedures to the study of the Na(+)-K(+)-ATPase protein. A wide array of information has become available about the kinetics, enzyme structure, and various conformational states as a result of the combined use of inhibitors, ligands, modifiers, and proteolytic enzymes. We will review a variety of reagents and approaches that have been employed to arrive at structure-function correlates and discuss critically the limits and ambiguities in the type of information obtained from these methodologies. Chemical modification of the Na(+)-pump protein has already provided a body of data and will, we anticipate, guide the efforts of mutagenesis studies in the future when suitable expression systems become available.