[The role of phosphorylase kinase subunits in interaction with glycogen].
The interaction of rabbit skeletal muscle phosphorylase kinase with CNBr-activated glycogen results in the formation of a covalent complex. The non-bound kinase was removed by chromatography on DEAE-cellulose and phenyl-Sepharose. The amount of the bound protein increased with an increase in the number of activated groups in the glycogen molecule; the enzyme activity was thereby decreased. The kinase covalently and non-covalently bound to glycogen exhibited a higher affinity for the protein substrate (phosphorylase b) as well as for Mg2+ and Ca2+ than did the kinase in the absence of glycogen. Electrophoresis performed under denaturating conditions showed that the gamma-subunit of phosphorylase kinase is responsible for the enzyme binding to CNBr-glycogen. The effect of cross-linking reagents (glutaric aldehyde, 1.5-difluoro-2.4-dinitrobenzene) on the binding of phosphorylase kinase subunits was studied. Glycogen afforded protection of the gamma-subunit from the cross-linking to other enzyme subunits. An analysis of the subunit composition of phosphorylase kinase covalently bound to CNBr-glycogen and of the enzyme treated with cross-linking reagents in the presence of glycogen-revealed that the gamma-subunit is involved in the specific binding of phosphorylase kinase to glycogen.
Shur
S A
SA
Zemskova
M A
MA
Vulfson
P L
PL
Skolysheva
L K
LK
D000818:Animals; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005976:Glutaral / Q000494:pharmacology; D006003:Glycogen / Q000378:metabolism*; D007202:Indicators and Reagents; D007700:Kinetics; D009132:Muscles / Q000378:metabolism; D010764:Phosphorylase Kinase / Q000378:metabolism*; D011817:Rabbits
D007202:Indicators and Reagents; D006003:Glycogen; D010764:Phosphorylase Kinase; D003488:Cyanogen Bromide; D005976:Glutaral
Rol' sub''edinits kinazy fosforilazy vo vzaimodeĭstii s glikogenom.