Coelution of the type II holoenzyme form of cAMP-dependent protein kinase with regulatory subunits of the type I form of cAMP-dependent protein kinase.

摘要: The types and subunit composition of cAMP-dependent protein kinases in soluble rat ovarian extracts were investigated. Results demonstrated that three peaks kinase activity could be resolved using DEAE-cellulose chromatography. Based on the sedimentation regulatory subunits sucrose density gradient centrifugation, identification 8-N3[32P]cAMP labeled RI RII column fractions by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Scatchard analysis cAMP-stimulated activation eluted activity, following conclusions drawn regarding activity: peak 1, eluting with less than or equal to 0.05 M potassium phosphate, consisted type I form kinase; 2, 0.065-0.11 free a II tetrameric holoenzyme; 3, 0.125 an apparent RIIC trimer, followed elution 0.15 phosphate RII. confirmed as authentic based upon their molecular weights autophosphorylation characteristics. more basic holoenzyme was not attributable ionic properties subunits, isoelectric points photolabeled location from dissociation respective holoenzymes cAMP. This is first report low salt RI, presence trimer tissue extract.