[Mechanism of activation of cAMP-dependent protein kinase. Covalent modification of the holoenzyme by cupric 1,10-phenanthroline].
Modification of the cAMP-dependent protein kinase holoenzyme from porcine brain by cupric-1,10-phenanthroline was studied. The formation of conjugates with Mr of 180,000 and 100,000 Da, whose stoichiometry coincides with that of holoenzymes R2C2 and RC, and of a conjugate with Mr of 85,000 Da corresponding to the catalytic subunit conjugate with the proteolytic fragment of the regulatory subunit (Mr = 39,000 Da) was demonstrated. The modified enzyme was activated by cAMP.
Abduragimov
A R
AR
Tiurkin
V V
VV
Kochetkov
S N
SN
Severin
E S
ES
D000818:Animals; D001921:Brain / Q000201:enzymology; D002384:Catalysis; D002848:Chromatography, DEAE-Cellulose; D003432:Cross-Linking Reagents / Q000378:metabolism / Q000494:pharmacology*; D000242:Cyclic AMP / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D066298:In Vitro Techniques; D008970:Molecular Weight; D010618:Phenanthrolines / Q000378:metabolism / Q000494:pharmacology*; D011494:Protein Kinases / Q000378:metabolism*; D013552:Swine
D003432:Cross-Linking Reagents; D010618:Phenanthrolines; D000242:Cyclic AMP; D011494:Protein Kinases; C025205:1,10-phenanthroline
Mekhanizm aktivatsii cAMP-zavisimoĭ proteinkinazy. Kovalentnaia modifikatsiia kholofermenta mednym kompleksom 1,10-fenantrolina.