Actions of glycogen synthase and phosphorylase of rabbit-skeletal muscle on modified glycogens.

The high reactivities exhibited by rabbit-muscle synthase and phosphorylase for unmodified glycogen-acceptors decrease progressively, presumably because of a large increase in apparent Km as the glycogen molecule is converted into its component maltosaccharide chains by the debranching enzyme, isoamylase. Elongation of the outer chains of glycogen acceptor also results in decreased reactivities of the two transglucosylases and this is shown, for phosphorylase acting in the direction of glucan synthesis, to be caused by a decrease in the Vmax of the reaction. A partial restoration of the degradative reactivity of phosphorylase by a limited alpha-amylolysis of the long outer-chains of modified glycogen suggests a role of cytoplasmic alpha-amylase in mammalian glycogen metabolism.