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- W2055983048 abstract "Abstract Phosphorylation of rabbit muscle glycogen synthase by cyclic AMP-dependent protein kinase results in the incorporation of 32 P into two major tryptic peptides (P-1 and P-2) which are identified by isoelectric focusing on polyacrylamide gel. When 32 P-labeled synthase is incubated with rabbit muscle phosphoprotein phosphatase both P-1 and P-2 are hydrolyzed. Incubation of 32 P-labeled synthase with human placental alkaline phosphatase results in a specific hydrolysis of P-1. Measurement of the increase in synthase activity ratio accompanied by the dephosphorylation of P-1 with human placental alkaline phosphatase and, subsequently, of P-2 with phosphoprotein phosphatase shows that both P-1 and P-2 affect the glucose-6-P dependency of the synthase." @default.
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- W2055983048 date "1980-01-01" @default.
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- W2055983048 title "Dephosphorylation of rabbit skeletal muscle glycogen synthase by phosphoprotein phosphatase and human placental alkaline phosphatase" @default.
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- W2055983048 doi "https://doi.org/10.1016/0006-291x(80)90387-3" @default.
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