Abstract
Glycogen from flight muscle of the blowfly, Phormia regina, has been characterized ultrastructurally and biochemically. In situ, glycogen is in the form of rosettes, which vary in size with diameters of up to 0.1 micro. Sedimentation analysis of pure glycogen, isolated by mild buffer extraction, reveals a polydisperse molecular weight spectrum, with larger particles having molecular weights of 100 million. Treatment of native glycogen with alkali, under conditions usual for the extraction of the polysaccharide from tissues, results in a 5- to 10-fold reduction in molecular weight, as well as a chemical alteration of the molecule. Flight muscle phosphorylase has a lower affinity for native than for alkali-treated glycogen. The maximum velocity of the enzyme is also lower with native substrate. The apparent K(m) for inorganic phosphate is higher with native glycogen as cosubstrate. These kinetic differences with native and partially degraded glycogen demonstrate the importance of using the natural substrate in studies of biochemical control mechanisms.