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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

Villar-Palasi, C.; Wei, S.H.

Proceedings of the National Academy of Sciences of the United States of America 67(1): 345-350

1970

ISSN/ISBN: 0027-8424
PMID: 4318782
DOI: 10.1073/pnas.67.1.345
Accession: 042680486
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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 Mg(2+). Phosphorylase b kinase activity increases greatly when the Mg(2+):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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Related References

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