Tissue expression and phylogenetic appearance of the beta and gamma subunits of GTP binding proteins.
Antibodies raised against the T-beta gamma dimer of bovine retinal transducin specifically bind to the beta and gamma subunits of transducin in calf retina. Tissues from different vertebrates, but not from invertebrates, contained a band comigrating with the beta subunit of transducin (T-beta) which was immunostained. This protein most likely corresponds to the beta subunit of GTP binding proteins of hormonal systems (G-beta). In non-retinal vertebrate membranes, the antibodies did not recognize the gamma subunits of G proteins whereas a band comigrating with bovine T-gamma was detected in frog or rat retina. Although T-beta was precipitated by the T-beta gamma antiserum, we failed to immunoprecipitate the G-beta from calf brain.
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D010856:Columbidae; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000032:analysis*; D006054:Goldfish; D006110:Grasshoppers; D007106:Immune Sera; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000378:metabolism; D011817:Rabbits; D011898:Ranidae; D051381:Rats; D012160:Retina / Q000032:analysis; D013045:Species Specificity; D014018:Tissue Distribution; D015293:Transducin
D007106:Immune Sera; D046911:Macromolecular Substances; D008565:Membrane Proteins; D019204:GTP-Binding Proteins; D015293:Transducin