Elution of the regulatory subunit of cAMP-dependent protein kinase Type I isozyme derived from epididymal fat within the type II isozyme chromatographic peak.
No cAMP-dependent protein kinase activity is found upon DEAE-cellulose chromatography of mouse fat extracts at the low salt concentration characteristic of the Type I isozyme. The RI detected in fat extracts by photoincorporation of the analog, 8-N3 [32P]cAMP, elutes within the high salt Type II isozyme peak. The multiple charge variants of this photolabeled RI which can be resolved by two-dimensional gel electrophoresis are similar to those of the histoptypically-related cultured cells, SV3T3 and 3T6, which do contain Type I kinase isozyme activity peaks. This high salt-eluting RI may be part of a Type I holoenzyme whose elution properties are altered by interactions with other substances present in the extract.
D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D001345:Autoradiography; D002848:Chromatography, DEAE-Cellulose; D000242:Cyclic AMP / Q000494:pharmacology*; D004822:Epididymis / Q000201:enzymology; D007527:Isoenzymes / Q000302:isolation & purification*; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism
D007527:Isoenzymes; D000242:Cyclic AMP; D011494:Protein Kinases