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Stimulating effect of phosphatidic acid on autophosphorylation of phosphorylase kinase.

Abstract：

:Autophosphorylation of phosphorylase kinase from rabbit skeletal muscle was stimulated by acidic phospholipids such as phosphatidic acid (PA), phosphatidylinositol, and phosphatidyl-serine. PA stimulated an initial velocity of autophosphorylation 3.8-fold. When fully autophosphorylated, about 11 mol of phosphate per tetramer (alpha beta gamma delta) were incorporated in the presence of PA and about 6.5 mol in the absence of PA. In the presence of PA (100 micrograms/ml), there was a concomitant enhancement of its kinase activity about 25-fold at pH 6.8. PA (100 micrograms/ml) sharply decreased an apparent Ka for Ca2+ on autophosphorylation from 4.0 X 10(-5) M to 1.0 X 10(-6) M. Available evidence indicates that the Ca2+-activated, PA-dependent autophosphorylation of phosphorylase kinase shows an ability to stimulate glycogen breakdown.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Negami AI,Sasaki H,Yamamura H

doi

10.1016/0006-291x(85)91296-3

subject

Has Abstract

pub_date

1985-09-16 00:00:00

pages

712-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)91296-3

journal_volume

131

pub_type

杂志文章

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