Properties of potassium activated p-nitrophenyl phosphatase of plasma membranes isolated from rat stomach muscle.

Abstract:

:The plasma membrane-enriched fraction isolated from smooth muscle of rat gastric fundus was found to contain a substantial level of potassium-stimulated p-nitrophenylphosphatase activity (K-pNPPase), and its subcellular distribution closely resembled that of other plasma membrane enzyme markers. The kinetic profile of K-pNPPase and its sensitivity toward ouabain and vanadate confirmed the identification of this activity with the partial reaction of the sodium pump. The specific activity of K-pNPPase and its sensitivity to ouabain was significantly increased in the presence of saponin, indicating that part of this activity is latent when assayed on native membrane preparation. K-pNNPase was sensitive to the presence of calcium ions in the assay medium. The Ca2+-inhibition of K-pNNPase was accompanied by increased sensitivity of the enzyme to ouabain. On the other hand, calmodulin and Ca antagonists had no effect on K-pNPPase activity nor its sensitivity to calcium.

journal_name

J Bioenerg Biomembr

authors

Kostka P,Kwan CY

doi

10.1007/BF00743050

subject

Has Abstract

pub_date

1986-08-01 00:00:00

pages

295-306

issue

4

eissn

0145-479X

issn

1573-6881

journal_volume

18

pub_type

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