The Kinetics of Glycogen Phosphorylases from Brain and Muscle

摘要: Abstract A kinetic study has been made of phosphorylase a from rabbit brain and b muscle. In the case data indicate strong cooperative interaction between glycogen phosphate sites adenylate sites. Under experimental conditions there was found little evidence sites, although few experiments under different work others, some is possible. Although are presumably at least two in active form enzyme, no sign one site with another or another. The behavior similar to that reported earlier for muscle except failure show phosphate-adenylate characteristic latter. enzyme also much greater affinity somewhat lower phosphate. more complicated than a. can be adequately explained by formulation involving binding each 5'-adenylate inorganic phosphate, glycogen. Random order addition indicated marked many Of 17 independent constants demanded this 10 have provisionally evaluated. pattern resembles but apparent affinities greater. Raising temperature 38° profoundly decreases all four enzymes glycogen, comparatively effect on