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Publication : Inverse relationship of skeletal muscle glycogen from wild-type and genetically modified mice to their phosphorylase a activity.

First Author  Schliselfeld LH Year  2002
Journal  Biochem Biophys Res Commun Volume  290
Issue  2 Pages  874-7
PubMed ID  11785984 Mgi Jnum  J:73924
Mgi Id  MGI:2157196 Doi  10.1006/bbrc.2001.6292
Citation  Schliselfeld LH, et al. (2002) Inverse relationship of skeletal muscle glycogen from wild-type and genetically modified mice to their phosphorylase a activity. Biochem Biophys Res Commun 290(2):874-7
abstractText  Leg muscle was biopsied and frozen for storage at -70 degrees C. from 5 wild-type mice, two knocked out acid alpha-glucosidase (GAA) gene mice, and seven glycogen synthase plus glucose muscle transporter transgenic mice. All of the wild-type mice had very little muscle glycogen (3.58 +/- 1.67 micromols glucosyl subunits per g muscle), and 52% or more of its glycogen phosphorylase activity without AMP (69% +/- 17% glycogen phosphorylase a). In contrast the GAA knockout and transgenic mice had glycogen ranging from 63 to 297 micromols glucosyl subunits per g muscle, and very little or no glycogen phosphorylase activity without 1.00 mM AMP (4.8% and less glycogen phosphorylase a). This suggests that there is an inverse relationship between mouse muscle phosphorylase a and the muscle's glycogen content.
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