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The functional unit of Na,K-ATPase is a monomeric alphabeta protomer.

Abstract：

:The ouabain-resistant and ouabain-sensitive alpha-subunit cRNAs in various molar ratios were injected into Xenopus oocytes together with cRNA for the beta-subunit. The ouabain-resistant ATPase activity, as well as ouabain-resistant Rb+ uptake, of the injected oocytes increased linearly with increasing the amount of cRNA for the ouabain-resistant alpha-subunit. When a functionless mutant was used instead of the ouabain-sensitive alpha-subunit, similar results were obtained in ATPase activity and Rb+ uptake. These results indicate that a monomeric alphabeta protomer is a functional unit of membrane-bound Na,K-ATPase, even if the enzyme exists structurally as a diprotomer or higher oligomers in membranes.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Takeda K,Kawamura M

doi

10.1006/bbrc.2001.4292

subject

Has Abstract

pub_date

2001-02-09 00:00:00

pages

1364-6

issue

5

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)94292-5

journal_volume

280

pub_type

杂志文章

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