[Kinetics of kinase phosphorylase action in a cascade enzymatic system. I. Theoretical basis of a method for determining phosphorylase kinase activity].
Based on a theoretical analysis of functioning of a monocascade enzymatic system, a method for continuous monitoring of the phosphorylase kinase-catalyzed enzymatic reaction has been developed. The method is based on the ability of the kinase reaction product--the phosphorylated form of glycogen phosphorylase (form a)-to catalyze glycogen phosphorolysis (with inorganic phosphate as the low molecular weight substrate) or synthesis (with glucose 1-phosphate) in the absence of AMP. A turbidimetric method may be used for the monitoring of the reaction of glycogen degradation (or synthesis) by phosphorylase a formed in the course of the kinase reaction. A method to calculate the initial rate of the kinase reaction from an absorbance versus (time)2 plot has been theoretically substantiated.
Kurganov
B I
BI
D000818:Animals; D002384:Catalysis; D006003:Glycogen / Q000378:metabolism; D007700:Kinetics; D008962:Models, Theoretical; D009132:Muscles / Q000201:enzymology; D010764:Phosphorylase Kinase / Q000378:metabolism*
D006003:Glycogen; D010764:Phosphorylase Kinase
Kinetika deĭstviia kinazy fosforilazy v kaskadnoĭ fermentnoĭ sisteme. I. Teoreticheskoe obosnovanie metoda opredeleniia fermentativnoĭ aktivnosti kinazy fosforilazy.