PROPERTIES OF A HIGH SPECIFIC ACTIVITY (NA+-K+)-STIMULATED ATPASE FROM RAT INTESTINAL MUCOSA

被引：35

作者：

QUIGLEY, JP

GOTTERER, GS

机构：

[1] Department of Physiological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 173卷 / 03期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0005-2736(69)90011-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A high specific activity, membrane-bound, (Na+-K+)-stimulated ATPase, isolatable in good yield from rat intestinal mucosal cells was examined for its enzymatic properties. The stimulated enzyme activity required the combined presence of Na+ and K+ in physiological concentrations and exhibited high sensitivity to K+ and an absolute requirement for Na+. A Mg2+/ATP ratio of 1.0 was necessary for optimal activity and the Km for ATP was 0.1 mM. ATP was the only nucleotide triphosphate hydrolyzed. The effect of amino acids, pH, ouabain, phloridzin and fluoride ion on the enzymatic activity was also examined. © 1969.

引用

页码：469 / &

共 27 条

[1]

ALVARADO F, 1962, BIOCHIM BIOPHYS ACTA, V56, P170, DOI 10.1016/0006-3002(62)90543-7

[2] CARDIAC (MICROSOMAL) NA + K ADENOSINETRIPHOSPHATASE AND ITS POSSIBLE RELATIONSHIP TO ACTIVE NA + K TRANSPORT SYSTEM [J].