A bacterial high-affinity GABA binding protein: isolation and characterization

Biochem Biophys Res Commun. 2000 Feb 5;268(1):65-8. doi: 10.1006/bbrc.1999.1960.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / metabolism
  • Binding, Competitive
  • Carrier Proteins / chemistry
  • Carrier Proteins / isolation & purification*
  • Carrier Proteins / metabolism
  • Mammals
  • Molecular Weight
  • Mutation
  • Pseudomonas fluorescens / genetics
  • Pseudomonas fluorescens / metabolism
  • Receptors, GABA-A / metabolism
  • gamma-Aminobutyric Acid / metabolism*

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Receptors, GABA-A
  • gamma-Aminobutyric Acid