Purification and characterization of subforms of the guanine‐nucleotide‐binding proteins Gαi and Gαo
- 1 August 1989
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 183 (3) , 687-692
- https://doi.org/10.1111/j.1432-1033.1989.tb21099.x
Abstract
Five different pertussis-toxin-sensitive guanine-nucleotide-binding proteins (G proteins) were purified from bovine brain. Immunochemical characterization of .alpha. subunits identified two G.alpha.O proteins (G.alpha.o-I and G.alpha.o-II), two 41-kDa G.alpha.i proteins (G.alpha.i-I and G.alpha.i-II) and the 40-kDa G.alpha.i2 protein. Site-directed antisera specific for G.alpha.o proteins did not differentiate between G.alpha.o-I and G.alpha.o-II. However, in situ peptide mapping using polyacrylamide gel electrophoresis revealed distinct cleavage products with different proteases for each of these proteins. Additionally comparison of Rf values demonstrated a slightly faster migration for G.alpha.o-II than for G.alpha.o-I, which is the only type of G.alpha.o protein present in cell membranes of the neuroblastoma/glioma cell line NG 108-15. The importance of these structural differences and possible functional implications are discussed.This publication has 27 references indexed in Scilit:
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