Glycogen synthase phosphatase of rat liver. Its separation from phosphorylase phosphatase on DE-52 columns. |
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Authors: | K Kikuchi S Tamura A Hiraga S Tsuiki |
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Affiliation: | Biochemistry Laboratory, Research Institute for Tuberculosis, Leprosy and Cancer, Tohoku University, Sendai 980, Japan |
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Abstract: | Glycogen synthase D was prepared from rat liver by chromatographing the glycogen pellet on DE-52 columns. It was free of glycogen and phosphorylase and converted readily into synthase I upon incubation with glycogen synthase phosphatase. With this synthase D as substrate, the identity of rat liver glycogen synthase phosphatase was studied by means of DE-52 column chromatography. Under the conditions developed, synthase phosphatase emerged from the columns as a sharp, single peak, and phosphorylase phosphatase came off later. The two phosphatases were also different from each other in stability, synthase phosphatase being less stable than phosphorylase phosphatase. |
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