Studies on interaction of phosphorylase kinase from rabbit skeletal muscle with glycogen in the presence of ATP and ADP.
The influence of ATP on complex formation of phosphorylase kinase (PhK) with glycogen in the presence of Ca(2+) and Mg(2+) has been studied. The initial rate of complex formation decreases with increasing ATP concentration, the dependence of the initial rate on the concentration of ATP having a cooperative character. Formation of the complex of PhK with glycogen in the presence of ATP occurs after a lag period, which increases with increasing ATP concentration. The dependence of the initial rate of complex formation (v) on the concentration of non-hydrolyzed ATP analogue, beta,gamma-methylene-ATP, follows the hyperbolic law. A correlation between PhK-glycogen complex formation and (32)P incorporation catalyzed by PhK itself and by the catalytic subunit of cAMP-dependent protein kinase has been shown. For ADP (the product and allosteric effector of the PhK reaction) the dependence of v on ADP concentration has a complicated form, probably due to the sequential binding of ADP at two allosteric sites on the beta subunit and the active site on the gamma subunit.
Andreeva
I E
IE
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky prospect, Moscow, Russia.
Makeeva
V F
VF
Livanova
N B
NB
Petukhov
S P
SP
Kurganov
B I
BI
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D004789:Enzyme Activation; D006003:Glycogen / Q000378:metabolism*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D018482:Muscle, Skeletal / Q000201:enzymology / Q000378:metabolism*; D009391:Nephelometry and Turbidimetry; D010764:Phosphorylase Kinase / Q000378:metabolism*; D010766:Phosphorylation; D011817:Rabbits
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006003:Glycogen; D010764:Phosphorylase Kinase; D008274:Magnesium; D002118:Calcium