A Bacterial High-Affinity GABA Binding Protein: Isolation and Characterization

A γ-aminobutyric acid (GABA) binding protein (GBP) was isolated from a bacterial mutant which has high-affinity GABA binding characteristics comparable with the GABAA brain receptor in mammals. The GBP was partially purified and characterized and was shown to be a periplasmic protein of approximatel...

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Bibliographic Details
Published in:	Biochemical and biophysical research communications Vol. 268; no. 1; pp. 65 - 68
Main Authors:	Guthrie, George D., Nicholson-Guthrie, Catherine S., Leary, H.Lee
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 05-02-2000
Subjects:	Animals Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Binding, Competitive Carrier Proteins - chemistry Carrier Proteins - isolation & purification Carrier Proteins - metabolism competitive binding assay g-Aminobutyric acid-binding protein GABA binding protein gamma-Aminobutyric Acid - metabolism Mammals Molecular Weight Mutation periplasmic protein Pseudomonas fluorescens - genetics Pseudomonas fluorescens - metabolism Receptors, GABA-A - metabolism molecular weight competitive binding assay GABA binding protein periplasmic protein
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Summary:	A γ-aminobutyric acid (GABA) binding protein (GBP) was isolated from a bacterial mutant which has high-affinity GABA binding characteristics comparable with the GABAA 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.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1999.1960