Title: Glycogen-synthase phosphatase activity in rat liver. Two protein components and their requirement for the activation of different types of substrate
Authors: Doperé, F ×
Vanstapel, Florent
Stalmans, Willy #
Issue Date: Jul-1980
Publisher: Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Series Title: European Journal of Biochemistry vol:104 issue:1 pages:137-46
Abstract: Three subfractions of glycogen synthase b (termed b1, b2, b3) have been isolated from the glycogen fraction of dog liver on the basis of a different affinity for DEAE-cellulose. Their kinetic properties and chromatographic behaviour are compatible with the presence of an increasing number of phosphorylated sites from synthase b1 towards b3. Synthase phosphatase activity in rat liver stems from two heat-labile and trypsin-labile proteins. These components are conveniently prepared from the cytosolic fraction of glycogen-depleted liver; the 'G-component' of the phosphatase co-sediments with added particulate glycogen, whereas the 'S-component' remains in the supernatant. The G-component alone did not convert any available synthase b to the a form. The synthase phosphatase activity of the S-component was variable according to the actual type of substrate. When acting on synthase b2 and b3, the S-component had a low phosphatase activity that was increased 7-fold and 11-fold, respectively, upon addition of the G-component. Synthase b1, however, was efficiently activated by the S-component, and only 35% faster in the presence of both components. When the cytosolic fraction of glycogen-depleted livers was analysed by sucrose-gradient centrifugation a single peak of phosphatase activity (S20, W = 10.2 S; provisional Mr = 254000) was detected with synthase b2 as substrate. In addition to this peak, presumably an S-G complex, synthase b1 also identified free S-component of lower and heterogeneous molecular weight. Our results illustrate in general the influence of the type of synthase b on the detection of synthase phosphatase activity, and specifically may provide an explanation for some discrepant reports on the subcellular distribution of the enzyme.
ISSN: 0014-2956
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Clinical Bacteriology and Mycology
Department of Cellular and Molecular Medicine - miscellaneous
Biomedical Quality Assurance Research Unit
× corresponding author
# (joint) last author

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