[Regulation of various isoenzymes of glutathione transferases of protein kinase A and cAMP].
Activation of purified glutathione transferase (CE 2.5.1.18) from the rabbit liver by cAMP-dependent protein kinase (protein kinase A) and activation of glutathione transferase from the rat liver and heart by cAMP preparations have been studied. A comparison of glutathione transferase activation on different substrates and the results of the inhibitor analysis of the activation phenomenon have shown that the second (mu) family of glutathione transferase isoenzymes (subunits, 3, 4, 6) is the most probable object of regulation. The first (alpha) family (subunits 1 and 2) and isoenzyme 5-5 are not probably regulated.
Kolesnichenko
L S
LS
Kulinskiĭ
V I
VI
Mantorova
N S
NS
D000818:Animals; D002395:Catecholamines / Q000378:metabolism; D000242:Cyclic AMP / Q000502:physiology*; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D011494:Protein Kinases / Q000502:physiology*; D011817:Rabbits; D013379:Substrate Specificity
D002395:Catecholamines; D007527:Isoenzymes; D000242:Cyclic AMP; D005982:Glutathione Transferase; D011494:Protein Kinases
Reguliatsiia razlichnykh izofermentov glutationtransferazy proteinkinazoĭ A i cAMP.