J Biol Chem. 1986 Jun 5;261(16):7393-9.

The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins.

Ferguson KM, Higashijima T, Smigel MD, Gilman AG.

Abstract

Purified guanine nucleotide-binding regulatory proteins, as either the oligomers or the isolated nucleotide-binding alpha subunits, display anomalous kinetics of nucleotide binding. This is due to the presence of tightly bound GDP in these preparations. The dissociation of bound GDP is the rate-limiting step for nucleotide binding. GDP can be removed by chromatography in the presence of 1 M (NH4)2SO4 and 20% glycerol, which yields preparations of G proteins that contain less than 0.1 mol of GDP/mol of guanosine 5'-(gamma-thio)triphosphate (GTP gamma S)-binding site. When the GDP is removed, the binding of GTP gamma S displays kinetics consistent with a bimolecular reaction.

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The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins.

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