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. 1970 Sep;67(1):345–350. doi: 10.1073/pnas.67.1.345

Conversion of Glycogen Phosphorylase b to a by Non-Activated Phosphorylase b Kinase: an In Vitro Model of the Mechanism of Increase in Phosphorylase a Activity with Muscle Contraction

C Villar-Palasi 1,2,*, S H Wei 1,2
PMCID: PMC283210  PMID: 4318782

Abstract

Phosphorylase b kinase activity, as present in resting muscle in the non-activated form, appears to be ample to account for the fast appearance of phosphorylase a observed with muscle contraction. The kinase activity is repressed by free ATP and stimulated by free Mg2+. Phosphorylase b kinase activity increases greatly when the Mg2+:ATP ration exceeds 1. It is proposed that the breakdown of ATP that occurs during muscle contraction may represent the triggering factor for the observed in vivo conversion of phosphorylase b into a.

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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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