Rapid activation-inactivation of liver uridine diphosphate glucose-glycogen transferase and phosphorylase by insulin and glucagon in vivo
JS Bishop, J Larner - Journal of Biological Chemistry, 1967 - Elsevier
JS Bishop, J Larner
Journal of Biological Chemistry, 1967•ElsevierInsulin administered in vivo activates dog liver uridine diphosphate glucose-glycogen
transferase within 7 to 13 min. It also inactivates phosphorylase. Glucagon reverses these
changes equally rapidly. Transferase I has an apparent K m for UDP-glucose which is
calculated to be 17-fold lower than that for transferase D. Interconversion of transferase D
and I activities in liver is suggested to occur and to be catalyzed by an enzymic system which
may be similar to that in muscle.
transferase within 7 to 13 min. It also inactivates phosphorylase. Glucagon reverses these
changes equally rapidly. Transferase I has an apparent K m for UDP-glucose which is
calculated to be 17-fold lower than that for transferase D. Interconversion of transferase D
and I activities in liver is suggested to occur and to be catalyzed by an enzymic system which
may be similar to that in muscle.
Insulin administered in vivo activates dog liver uridine diphosphate glucose-glycogen transferase within 7 to 13 min. It also inactivates phosphorylase. Glucagon reverses these changes equally rapidly. Transferase I has an apparent Km for UDP-glucose which is calculated to be 17-fold lower than that for transferase D. Interconversion of transferase D and I activities in liver is suggested to occur and to be catalyzed by an enzymic system which may be similar to that in muscle.
Elsevier