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. 1991 Aug 15;278(Pt 1):113–117. doi: 10.1042/bj2780113

The expression of glycogen phosphorylase in normal and dystrophic muscle.

D M Leyland 1, R J Beynon 1
PMCID: PMC1151456  PMID: 1883323

Abstract

Specific cofactor labelling was employed to determine the degradation rate of glycogen phosphorylase in normal adult C57BL/6J mice and their dystrophic counterparts (C57BL/6Jdy/dy). The rate constant for the decay of phosphorylase-bound label was 0.125 day-1 in normal muscle and 0.49 day-1 in dystrophic muscle, i.e. a lower rate of catabolism of phosphorylase in dystrophic muscle. Quantitative Northern-blot analyses of total RNA isolated from normal and dystrophic muscle indicated that the abundance of phosphorylase mRNA as a percentage of total RNA was approx. 40% lower in dystrophic muscle. The specific activity of phosphorylase in dystrophic muscle is approx. 60% lower than in normal muscle, and is elicited by a lower rate of turnover of the enzyme, i.e. both synthesis and degradation are decreased.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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