Literature DB >> 3034285

The GABAA receptor and its antibodies.

F A Stephenson, C Mamalaki, S O Casalotti, E A Barnard.   

Abstract

The GABAA/benzodiazepine receptor has been purified to homogeneity from bovine and rat cerebral cortex. Under optimum conditions, the purified receptor has been shown to possess four distinct drug-binding sites, for GABA, benzodiazepine, barbiturate and Cl- channel gating classes of ligands. The receptor is a multi-subunit membrane glycoprotein with an oligomeric size of 230,000 Da. It contains at least two subunits, alpha and beta, the first of which can be photoaffinity-labelled with the benzodiazepine, flunitrazepam. Polyclonal and monoclonal antibodies have been raised to the native receptor and both have been used in an immunological characterization of the receptor protein in detergent extracts and likewise in purified preparations from bovine cerebral cortex.

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Year:  1986        PMID: 3034285

Source DB:  PubMed          Journal:  Biochem Soc Symp        ISSN: 0067-8694


  3 in total

1.  Mapping the benzodiazepine photoaffinity-labelling site with sequence-specific gamma-aminobutyric acidA-receptor antibodies.

Authors:  F A Stephenson; M J Duggan
Journal:  Biochem J       Date:  1989-11-15       Impact factor: 3.857

Review 2.  Understanding the GABAA receptor: a chemically gated ion channel.

Authors:  F A Stephenson
Journal:  Biochem J       Date:  1988-01-01       Impact factor: 3.857

3.  The GABAA/benzodiazepine receptor is a heterotetramer of homologous alpha and beta subunits.

Authors:  C Mamalaki; F A Stephenson; E A Barnard
Journal:  EMBO J       Date:  1987-03       Impact factor: 11.598

  3 in total

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