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

K. M. Ferguson, T. Higashijima, M. D. Smigel, A. G. Gilman

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186 Scopus citations

Abstract

Purified guanine nucleotide-binding regulatory proteins, as either the oligomers or the isolated nucleotide-binding α 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'-(γ-thio)triphosphate (GTPγS)-binding site. When the GDP is removed, the binding of GTPγS displays kinetics consistent with a bimolecular reaction.

Original languageEnglish (US)
Pages (from-to)7393-7399
Number of pages7
JournalJournal of Biological Chemistry
Volume261
Issue number16
StatePublished - Dec 1 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Ferguson, K. M., Higashijima, T., Smigel, M. D., & Gilman, A. G. (1986). The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins. Journal of Biological Chemistry, 261(16), 7393-7399.