title: A bacterial high-affinity GABA binding protein: isolation and characterization.
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.
authors.affiliation: Department of Biochemistry, Indiana University School of Medicine, 700 Drexel Drive, Evansville, Indiana, 47712-9629, USA. gguthrie@usi.edu
authors.forename: G D
authors.initials: GD
authors.lastname: Guthrie
authors.forename: C S
authors.initials: CS
authors.lastname: Nicholson-Guthrie
authors.forename: H L
authors.initials: HL
authors.lastname: Leary
mesh_terms: 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*
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D011963:Receptors, GABA-A; D005680:gamma-Aminobutyric Acid