Liver glycogen synthase phosphatase and phosphorylase phosphatase activities in vitro following glucose and glucagon administration

frank q Nuttall, Daniel P. Gilboe

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Correlation of the changes in phosphorylase a concentration with the synthase phosphatase velocity in a glycogen particle preparation in the presence of EDTA revealed that the initial synthase phosphatase rate was greatest in extracts from glucose-treated rats and least in extracts from glucagon-treated rats. In all cases the velocity increased with time and with a decrease in phosphorylase a. However, a threshold release of phosphatase activity when phosphorylase a reached a critical level was not observed. The data are compatible with either an independent regulation of synthase phosphatase by glucose and glucagon or regulation of the activity by phosphorylase over a range of phosphorylase a concentrations.

Original languageEnglish (US)
Pages (from-to)483-486
Number of pages4
JournalArchives of Biochemistry and Biophysics
Volume203
Issue number1
DOIs
StatePublished - Jan 1 1980

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