作者: S L Weldon , M C Mumby , S S Taylor
DOI: 10.1016/S0021-9258(18)88992-X
关键词:
摘要: Although the major form of soluble cAMP-dependent protein kinase in bovine cerebral cortex can be classified as a type II kinase, regulatory subunit (RII) distinguished from RII found other tissues such heart. Heart and brain were qualitatively by autophosphorylation followed sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The mobility dephosphorylated heart shifted an apparent Mr 55,000 to 57,000 following autophosphorylation. In contrast, when purified was autophosphorylated with [gamma-32P]ATP, two radiolabeled bands visualized, minor band (less than or equal 20%) which migrated similar = did not shift its response Brain further on basis cAMP binding. Millipore filtration equilibrium dialysis indicated that 2 mol bound/mol contrast 4 mol/mol RII. Immunological differences also apparent. Radioimmunoassays using monoclonal antibodies showed had less 4% cross-reactivity Both immunoblotting immunoprecipitation well serum established phosphorylated associated exclusively component behaved like lack neural different targeted hinge region area where structural might anticipated, comparative sequence analysis this definitively is unique gene product expressed