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- W1531545561 abstract "This chapter discusses measurement of receptor-stimulated guanosine 5'-O-(γ-Thio)triphosphate binding by G Proteins. Many transmembrane signaling processes caused by extracellular hormones and neurotransmitters are mediated by receptors interacting with heterotrimeric (αβγ) guanine nucleotide-binding proteins (G proteins) attached to the inner face of the plasma membrane. Agonist-liganded receptors apparently initiate activation of G proteins by catalyzing the exchange of guanosine 5'-diphosphate (GDP) by guanosine 5'-triphosphate (GTP) bound to the α subunits. In membrane preparations and reconstituted systems, this activation process is frequently monitored by studying agonist stimulation of high-affinity GTPase, an enzymatic activity of G-protein α subunits. To study the initial steps of G-protein activation by agonist-liganded receptors in a quantitative manner, the binding of radiolabeled GTP analogs, which are not hydrolyzed by the GTPase activity of G-protein α subunits, to G proteins is determined. Of these GTP analogs, guanosine 5'-O-(γ-[35S]thio)triphosphate ([35S]GTPγS) is most frequently used. This nucleotide has a high affinity for all types of G proteins and is available with a relatively high specific radioactivity (1000-1400 Ci/mmol; physical half-life 87.4 days). The chapter describe the measurement of receptor induced binding of [35S]GTPγS to membranous and detergent-solubilized G proteins and how this method can be adapted to different G proteins for an optimal response to receptor stimulation." @default.
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- W1531545561 date "1994-01-01" @default.
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- W1531545561 title "[1] Measurement of receptor-stimulated guanosine 5′-O-(γ-thio)triphosphate binding by G proteins" @default.
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- W1531545561 doi "https://doi.org/10.1016/s0076-6879(94)37048-6" @default.
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