[Interaction of muscle glycogen phosphorylase B with F-actin].
The binding of rabbit muscle glycogen phosphorylase b to F-actin has been studied by sedimentation in analytical centrifuge in 10 mM Tris-acetate buffer pH 6.8 at 20 degrees C. The adsorption capacity of F-actin is equal to (7.8 +/- 0.9) X 10(-7) mole of glycogen phosphorylase b per 1 g of F-actin; the microscopic dissociation constant for the glycogen phosphorylase-F-actin complex is (5.4 +/- 0.5) X 10(-7) M. It was found that the allosteric activator, AMP, facilitates the adsorption of glycogen phosphorylase b on F-actin, whereas the substrate, Pi, and the inhibitor, ATP, cause an opposite effect.
Chebotareva
N A
NA
Sugrobova
N P
NP
Ostrovskaia
M V
MV
Livanova
N B
NB
Poglazov
B F
BF
D000199:Actins / Q000378:metabolism*; D000327:Adsorption; D000818:Animals; D001665:Binding Sites; D066298:In Vitro Techniques; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity
D000199:Actins; D010763:Phosphorylase b; D006005:Phosphorylases
Vzaimodeĭstvie myshechnoĭ glikogenfosforilay B s F-aktinom.