This item still needs to be validated !
Title: The catalytic activity of phosphorylase b in the liver. With a note on the assay in the glycogenolytic direction
Authors: Stalmans, Willy
Gevers, G #
Issue Date: Jun-1982
Series Title: The Biochemical journal. vol:200 issue:2 pages:327-36
Abstract: 1. The activity and the kinetic properties of purified hepatic phosphorylases a and b from rabbit and rat have been investigated in the glycogenolytic direction with a radiochemical assay. 2. In contrast with the a form, phosphorylase b has an absolute requirement for both AMP and a lyotropic salt. When the latter effectors are included, the b/a-form activity ratio remains low (0.03-0.15) at the hepatic concentration of Pi, because the b form has an exceedingly low affinity for this substrate. 3. Only phosphorylase b is significantly inhibited by glucose, glucose 6-phosphate and MgATP2-. Assays in the presence of substrastes, stimulators and inhibitors in the physiological concentration range indicate that glycogenolysis in the liver depends strictly on the conversion of phosphorylase b into a. Even at 1 mM-AMP the b/a-form activity ratio does not exceed 0.01. 4. Current spectrophotometric procedures for the glycogenolytic assay of phosphorylase in crude liver preparations are highly specific for the a form; the measurement of total phosphorylase (a + b) would require impractical modifications, and is better performed in the direction of glycogen synthesis.
ISSN: 0264-6021
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Cellular and Molecular Medicine - miscellaneous
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science