Dephosphorylation of rabbit skeletal muscle glycogen synthase by phosphoprotein phosphatase and human placental alkaline phosphatase |
| |
Authors: | K P Huang F L Huang |
| |
Affiliation: | 1. National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20205 USA;2. Department of Preventive Medicine and Biometrics, Uniformed Services University of Health Sciences, Bethesda, MD 20014 USA |
| |
Abstract: | Phosphorylation of rabbit muscle glycogen synthase by cyclic AMP-dependent protein kinase results in the incorporation of 32P into two major tryptic peptides (P-1 and P-2) which are identified by isoelectric focusing on polyacrylamide gel. When 32P-labeled synthase is incubated with rabbit muscle phosphoprotein phosphatase both P-1 and P-2 are hydrolyzed. Incubation of 32P-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. |
| |
Keywords: | The author to whom all inquiries should be addressed. |
本文献已被 ScienceDirect 等数据库收录! |
|