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Updated: Aug 2, 2026
Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking
Published on: March 28, 2014
A bacterial high-affinity GABA binding protein: isolation and characterization
G D Guthrie1, C S Nicholson-Guthrie, H L Leary
1Department of Biochemistry, Indiana University School of Medicine, 700 Drexel Drive, Evansville, Indiana, 47712-9629, USA. gguthrie@usi.edu
Abstract:
A gamma-aminobutyric acid (GABA) binding protein (GBP) was isolated from a bacterial mutant which has high-affinity GABA binding characteristics comparable with the GABA(A) brain receptor in mammals. The GBP was partially purified and characterized and was shown to be a periplasmic protein of approximately 42,000 molecular weight. To determine the molecular weight, a bacterial GABA binding assay was used with SDS-PAGE. This procedure did not require large amounts or complete purification of protein and may be useful as a simple method in estimating the molecular weight of other bacterial binding proteins.
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