A bacterial high-affinity GABA binding protein: isolation and characterization.
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.
Guthrie
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Department of Biochemistry, Indiana University School of Medicine, 700 Drexel Drive, Evansville, Indiana, 47712-9629, USA. gguthrie@usi.edu
Nicholson-Guthrie
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Leary
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D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008322:Mammals; D008970:Molecular Weight; D009154:Mutation; D011551:Pseudomonas fluorescens / Q000235:genetics / Q000378:metabolism; D011963:Receptors, GABA-A / Q000378:metabolism; D005680:gamma-Aminobutyric Acid / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D011963:Receptors, GABA-A; D005680:gamma-Aminobutyric Acid