An investigation of bombesin/gastrin-releasing peptide-receptor-G-protein coupling in rat brain membranes

1989 ◽  
Vol 17 (2) ◽  
pp. 410-411
Author(s):  
HELEN WISE ◽  
KEITH P. RAY
Keyword(s):  
Rat Brain ◽  
G Protein ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Peptide Receptor ◽  
Gastrin Releasing Peptide ◽  
Brain Membranes ◽  
Rat Brain Membranes

Glycosylation of the Gastrin-Releasing Peptide Receptor and Its Effect on Expression, G Protein Coupling, and Receptor Modulatory Processes

2000 ◽  
Vol 58 (6) ◽  
pp. 1490-1501 ◽  
Author(s):  
Richard V. Benya ◽  
Takashi Kusui ◽  
Tatsuro Katsuno ◽  
Takaharu Tsuda ◽  
Samuel A. Mantey ◽  
...  
Keyword(s):  
G Protein ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Peptide Receptor ◽  
Gastrin Releasing Peptide

Increased baclofen-stimulated G protein coupling and deactivation in rat brain cortex during development

2004 ◽  
Vol 151 (1-2) ◽  
pp. 67-73 ◽  
Author(s):  
Jiri Stöhr ◽  
Lenka Bourova ◽  
Lucie Hejnova ◽  
Ivanna Ihnatovych ◽  
Jiri Novotny ◽  
...  
Keyword(s):  
Rat Brain ◽  
G Protein ◽  
Brain Cortex ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Rat Brain Cortex

scholarly journals Purification of the G-protein G13 from rat brain membranes

1994 ◽  
Vol 303 (1) ◽  
pp. 135-140 ◽  
Author(s):  
R Harhammer ◽  
B Nürnberg ◽  
K Spicher ◽  
G Schultz
Keyword(s):  
Rat Brain ◽  
G Protein ◽  
G Proteins ◽  
Gradient Centrifugation ◽  
Sucrose Density Gradient ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Sucrose Density Gradient Centrifugation ◽  
Brain Membranes ◽  
Rat Brain Membranes

Significant amounts of G13, a member of the recently described G12-subfamily of heterotrimeric G-proteins, have been detected in rat brain membranes by specific antisera. The alpha-subunits of G13 (G alpha 13) were purified by using a combination of conventional and subunit-exchange chromatography. Purification was facilitated by the fact that the initial anion-exchange chromatography separated G13 from most of the other G-proteins, including Gq/11. Moreover, G alpha 13-enriched fractions obtained from this chromatographic step were devoid of beta gamma-dimers, despite the absence of G-protein-activating agents. Nevertheless, the purified G alpha 13 retained its ability to interact with beta gamma-dimers under appropriate conditions, i.e. the addition of Lubrol PX instead of cholate as detergent and the omission of ethylene glycol routinely used as a protecting additive. The interaction was demonstrated by (i) the binding of G alpha 13 to immobilized beta gamma-complexes and (ii) the formation of stable heterotrimers during sucrose-density-gradient centrifugation. Furthermore, our studies on G alpha 13 provide evidence for an extremely slow basal GDP/GTP exchange rate. The purified protein showed negligible binding of guanosine 5′-[gamma-[35S]thio]triphosphate (GTP[35S]). Accordingly, dissociation of G alpha 13 from immobilized beta gamma-complexes was achieved by AlF4-/Mg2+, but not by GTP[S]. These data indicate that G13 exhibits properties highly distinct from those of other G-proteins.

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