Association of two pertussis toxin-sensitive G-proteins with the D2-dopamine receptor from bovine striatum - PubMed (original) (raw)

Association of two pertussis toxin-sensitive G-proteins with the D2-dopamine receptor from bovine striatum

Z Elazar et al. EMBO J. 1989 Aug.

Abstract

The solubilized D2-dopamine receptor from bovine striatum exhibits high and low affinity states for dopaminergic agonists. Guanine nucleotides and pertussis toxin convert the solubilized receptor from a high affinity state to a low one. A D2-receptor preparation partially purified by affinity chromatography on a haloperidol adsorbent, exhibited agonist-stimulated GTPase activity. [32P]ADP-ribosylation by pertussis toxin of this receptor preparation resulted in the specific labeling of two protein bands corresponding to mol. wts of 39 and 41 kd, in SDS-PAGE. Association of these G-proteins with the receptor was specifically inhibited by Gpp(NH)p. Immunoblot analysis of these G-proteins indicated that the 41- and 39-kd protein bands are analogous to brain Gi and Go respectively. These experiments demonstrate that two distinct pertussis toxin-sensitive G-proteins are functionally associated with bovine striatum D2-dopamine receptor.

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References

1. 1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
2. 1. Proc Natl Acad Sci U S A. 1986 Apr;83(7):2258-62 - PubMed
3. 1. J Biol Chem. 1983 Apr 25;258(8):4957-65 - PubMed
4. 1. J Neural Transm Suppl. 1983;18:139-47 - PubMed
5. 1. Proc Natl Acad Sci U S A. 1984 Apr;81(8):2553-7 - PubMed

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