Accelerated degradation of glycogen phosphorylase in denervated and dystrophic mouse skeletal muscle

Author:

Butler P. Elaine12,Cookson E. Jane1,Beynon Robert J.1

Affiliation:

1. Department of Biochemistry, University of Liverpool, PO Box 147, Liverpool L69 3BX, UK

2. Department of Biochemistry, Virginia Commonwealth University, Richmond VA 23298, USA

Abstract

Pyridoxal phosphate, the cofactor of glycogen phosphorylase, fulfils the criteria needed of a turnover label for this enzyme. The decay of protein-bound label following administration of [3H]pyridoxine is a good index of the rate of degradation of the enzyme in vivo. This method has been applied to the study of catabolism of the enzyme in normal, denervated and dystrophic mouse skeletal muscle. In both of the pathological conditions the enzyme is degraded more rapidly than normal.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

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