Elution of the catalytic subunits of the type I and type II forms of cyclic AMP-dependent protein kinase within the type I chromatographic peak.
The purpose of this investigation was to determine the elution location upon ion-exchange chromatography of the catalytic subunits of both the type I and type II isozyme forms of cAMP-dependent protein kinase. We show that ion-exchange chromatography with DEAE-Sepharose CL-6B yields an apparent type I chromatographic peak of cAMP-dependent protein kinase which can represent not only type I holoenzyme activity but also catalytic activity derived from either the type I or type II enzyme forms. Such knowledge of the elution location of the dissociated catalytic subunits can prevent incorrect identification of the distribution of cAMP-dependent protein kinase isozymes in studies which estimate the isozyme concentrations based on the relative proportions of the kinase activity peaks.
D000345:Affinity Labels; D000818:Animals; D001345:Autoradiography; D002384:Catalysis; D002852:Chromatography, Ion Exchange / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005612:Freeze Drying; D007527:Isoenzymes / Q000302:isolation & purification*; D008297:Male; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D011494:Protein Kinases / Q000302:isolation & purification*; D051381:Rats
D000345:Affinity Labels; D007527:Isoenzymes; D011494:Protein Kinases