Immunological crossreactivity of G-protein beta subunit and receptors for activated C-kinase.
Selective antisera against: 1) RACKs, 2) a putative common PKC-binding domain (peptide I), and 3) G-protein subunits, were used for immunoblot analysis with recombinant purified beta 1 gamma 2 subunits and a crude preparation of RACKs. Antipeptide I recognized not only RACKs but also the G-protein beta subunit. In addition, two RACK-specific antisera immunoreacted with the G-protein beta subunit. Similarly, anti-G beta comm and S-217 (beta gamma-specific antiserum) crossreacted with RACKs. Using an overlay assay, it was observed that proteins immunoprecipitated with anti-RACKs or with anti-G beta antisera bound activated PKC.
Departamento de Bioenergética, Facultad de Medicina, Universidad Nacional Autónoma de México, México D. F.
M
M
Robles-Flores
J A
JA
García-Sáinz
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000276:immunology*; D003429:Cross Reactions; D004789:Enzyme Activation; D019204:GTP-Binding Proteins / Q000276:immunology*; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D011493:Protein Kinase C / Q000378:metabolism*; D011817:Rabbits; D051381:Rats
D002352:Carrier Proteins; D011493:Protein Kinase C; D019204:GTP-Binding Proteins