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- W2014602384 abstract "The distribution of glycogen synthetase, phosphorylase, and amylo-1,6-glucosidase in subcellular fractions was studied in human and rabbit skeletal muscle. All glycogen synthetase and 60–70% of phosphorylase and amylo-l,6-glucosidase were sedimented with the microsome-glycogen fraction. These enzymes were redistributed to the final supernatant when glycogen was either digested by glucamylase or metabolically utilized in vitro, and the process was reversed by the addition of glycogen. Redistribution of the enzymes to the final supernatant also followed depletion of glycogen by sustained tetanus in vivo. When glycogen was separated from microsomes by filtration, the enzymes passed through the filter with glycogen. These results suggest that the principal enzymes of glycogen synthesis and degradation are bound to the polysaccharide rather than to membranes of the sarcoplasmic reticulum." @default.
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- W2014602384 title "Binding of enzymes of glycogen metabolism to glycogen in skeletal muscle" @default.
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- W2014602384 doi "https://doi.org/10.1016/0003-9861(71)90494-2" @default.
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