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Synergistically stimulated (Na+,K+)-adenosine triphosphatase from plasma membrane of a marine diatom.

Abstract：

:An ATP-hydrolyzing activity with the properties of a Mg(2+)-dependent (Na(+),K(+))-ATPase (ATP phosphohydrolase, EC 3.6.1.3) from a 20-fold purified plasma membrane fraction of the marine diatom, Nitzschia alba is described. The basal activity requires Mg(2+) and further stimulation by Na(+) or Na(+) plus K(+) is dependent on the presence of Mg(2+); Mn(2+) or Co(2+) can partially substitute for the divalent cation requirement but Ca(2+) equimolar with Mg(2+) inhibits the activity by 54%. ATP is the preferred substrate for the Na(+) plus K(+) stimulated activity, while CTP, UTP, and ADP are only slightly hydrolyzed. The apparent K(m) is 8 x 10(-4) M ATP. The ATP hydrolysis-rate is dependent on the relative concentrations of Na(+) and K(+); the K(0.5) for Na(+) and K(+) are 2 mM and 50 mM, respectively. Basal activity is synergistically stimulated by Na(+) plus K(+) only at certain ion concentrations and shows a strong specificity for both cations. In the presence of Na(+) at 5 mM and K(+) at 350 mM, the ATPase is completely inhibited by p-chloromercuric benzoic acid 10(-4) M, N-ethyl maleimide 10(-3) M, and iodoacetamide 10(-2) M, but is insensitive to ouabain at 10(-7) to 10(-3) M. This study demonstrates for the first time that algal plasma membrane contains an ATPase that is synergistically stimulated by Na(+) and K(+).

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Sullivan CW,Volcani BE

doi

10.1073/pnas.71.11.4376

subject

Has Abstract

pub_date

1974-11-01 00:00:00

pages

4376-80

issue

11

eissn

0027-8424

issn

1091-6490

journal_volume

71

pub_type

杂志文章

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