Affordable Access

Publisher Website

Evidence for protein phosphorylation as a regulatory mechanism for hepatic microsomal glucose 6 phosphatase

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
103
Issue
3
Identifiers
DOI: 10.1016/0006-291x(81)90912-8
Disciplines
  • Biology

Abstract

Abstract Incubation of microsomal vesicles with ATP and protein kinase results in a fivefold increased glucose-6-phosphatase activity. Evidence is presented that this effect is mediated via a moiety of the outer membrane surface. Evidence is also presented for the presence of an endogenous, peripheral membrane protein also capable of activating glucose-6-phosphatase in an ATP dependent reaction. It is suggested that the glucose-6-phosphate transmembrane carrier system may be the target of phosphorylation.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Evidence for protein phosphorylation as a regulato...

on Biochemical and Biophysical Re... Dec 15, 1981

A critical evaluation of the possible modulation o...

on Biochemical and Biophysical Re... August 1982

A critical evaluation of the possible modulation o...

on Biochemical and Biophysical Re... Jan 01, 1982

The ontogeny of human hepatic microsomal glucose-6...

on Clinical Chemistry September 1990
More articles like this..