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Promiscuity of GABAA‐receptor β3 subunits as demonstrated by their presence in α1, α2 and α3 subunit‐containing receptor subpopulations

Polyclonal antibodies were raised in rabbits against the GABAA‐receptor β3 subunit peptide sequence, KQSMPREGHGRHMDR‐NH2 coupled to keyhole limpet haemocyanin. These anti‐β3 379–393 antibodies immunoprecipitated in a dose‐dependent manner specific benzodiazepine agonist binding sites from Na+ deoxyc...

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Published in:	FEBS letters 1991-12, Vol.295 (1-3), p.81-83
Main Authors:	Pollard, Simon, Duggan, Michael J., Stephenson, F.Anne
Format:	Article
Language:	English
Subjects:	Aminoacid receptors (glycine, glutamate, gaba) Antibody Benzodiazepine Biological and medical sciences Cell receptors Cell structures and functions ELISA enzyme linked immunoadsorbent assay Fundamental and applied biological sciences. Psychology GABA GABAA Immunoaffinity keyhole limpet haemocyanin KLH Molecular and cellular biology Purification Receptor SDS-PAGE sodium dodecyl sulphate polyacrylamide gel electrophoresis γ-aminobutyric acid
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container_issue	1-3
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container_title	FEBS letters
container_volume	295
creator	Pollard, Simon Duggan, Michael J. Stephenson, F.Anne
description	Polyclonal antibodies were raised in rabbits against the GABAA‐receptor β3 subunit peptide sequence, KQSMPREGHGRHMDR‐NH2 coupled to keyhole limpet haemocyanin. These anti‐β3 379–393 antibodies immunoprecipitated in a dose‐dependent manner specific benzodiazepine agonist binding sites from Na+ deoxycholate extracts of bovine cerebral cortex. In immunoblots, anti‐β3 379–393 antibodies recognised two species with M fr 59 900 and M fr 57 200 in all preparations tested, which included crude detergent‐solubilised, benzodiazepine affinity chromatography‐purified receptor, anti‐α1 324–341 antibody, anti‐Cys α2 414–424 antibody and anti‐Cys α3 454–467 antibody immunoaffinity‐purified GABAA‐receptor subpopulations. These results provide evidence for the ubiquity and promiscuity of the GABAA‐receptor β3 subunit.
doi_str_mv	10.1016/0014-5793(91)81390-T
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These anti‐β3 379–393 antibodies immunoprecipitated in a dose‐dependent manner specific benzodiazepine agonist binding sites from Na+ deoxycholate extracts of bovine cerebral cortex. In immunoblots, anti‐β3 379–393 antibodies recognised two species with M fr 59 900 and M fr 57 200 in all preparations tested, which included crude detergent‐solubilised, benzodiazepine affinity chromatography‐purified receptor, anti‐α1 324–341 antibody, anti‐Cys α2 414–424 antibody and anti‐Cys α3 454–467 antibody immunoaffinity‐purified GABAA‐receptor subpopulations. 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These results provide evidence for the ubiquity and promiscuity of the GABAA‐receptor β3 subunit.</description><subject>Aminoacid receptors (glycine, glutamate, gaba)</subject><subject>Antibody</subject><subject>Benzodiazepine</subject><subject>Biological and medical sciences</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>ELISA</subject><subject>enzyme linked immunoadsorbent assay</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GABA</subject><subject>GABAA</subject><subject>Immunoaffinity</subject><subject>keyhole limpet haemocyanin</subject><subject>KLH</subject><subject>Molecular and cellular biology</subject><subject>Purification</subject><subject>Receptor</subject><subject>SDS-PAGE</subject><subject>sodium dodecyl sulphate polyacrylamide gel electrophoresis</subject><subject>γ-aminobutyric acid</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNo9UEFOwzAQtBBIlMIPOPjAASQCduzE8TGt2oKEBIdwthzHAaPUiexEKDd-AF-Bh_QRvISkRb3saGdmZ6UB4ByjG4xwfIsQpkHEOLnk-CrBhKMgOwATnDASEBonh2CytxyDE-_f0LAnmE_A55Or18arzrQ9rEu4Smdp-vvx5bTSTVs7uPkh0Hd5Z03rofSw0Ova-tbJVhcw72H7qo2DjdNeW6WhsXDzja-HEUJpiwH350Oqqm0rjTX2Be4fDGpTN10lWzMEn4KjUlZen_3jFDwvF9n8Lnh4XN3P04egwTHKgkLxMlcYEUqKUJY0jnPJKAlJSSmOWYSjPNQJySVCCaM8ZLyQEkWcEFWwpGRkCi52uY30Slalk1YZLxpn1tL1IkKcspgOtuXO9m4q3e9ljMRYvBhbFWOrgmOxLV5kYrmYhaMw8hxv2Yz8AezcgUs</recordid><startdate>19911216</startdate><enddate>19911216</enddate><creator>Pollard, Simon</creator><creator>Duggan, Michael J.</creator><creator>Stephenson, F.Anne</creator><general>Elsevier</general><scope>IQODW</scope></search><sort><creationdate>19911216</creationdate><title>Promiscuity of GABAA‐receptor β3 subunits as demonstrated by their presence in α1, α2 and α3 subunit‐containing receptor subpopulations</title><author>Pollard, Simon ; Duggan, Michael J. ; Stephenson, F.Anne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p160T-dc9fbc10343d2af466ba74323f44167515b2e83ba008749279daa05933cd78f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Aminoacid receptors (glycine, glutamate, gaba)</topic><topic>Antibody</topic><topic>Benzodiazepine</topic><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>ELISA</topic><topic>enzyme linked immunoadsorbent assay</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GABA</topic><topic>GABAA</topic><topic>Immunoaffinity</topic><topic>keyhole limpet haemocyanin</topic><topic>KLH</topic><topic>Molecular and cellular biology</topic><topic>Purification</topic><topic>Receptor</topic><topic>SDS-PAGE</topic><topic>sodium dodecyl sulphate polyacrylamide gel electrophoresis</topic><topic>γ-aminobutyric acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pollard, Simon</creatorcontrib><creatorcontrib>Duggan, Michael J.</creatorcontrib><creatorcontrib>Stephenson, F.Anne</creatorcontrib><collection>Pascal-Francis</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pollard, Simon</au><au>Duggan, Michael J.</au><au>Stephenson, F.Anne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Promiscuity of GABAA‐receptor β3 subunits as demonstrated by their presence in α1, α2 and α3 subunit‐containing receptor subpopulations</atitle><jtitle>FEBS letters</jtitle><date>1991-12-16</date><risdate>1991</risdate><volume>295</volume><issue>1-3</issue><spage>81</spage><epage>83</epage><pages>81-83</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Polyclonal antibodies were raised in rabbits against the GABAA‐receptor β3 subunit peptide sequence, KQSMPREGHGRHMDR‐NH2 coupled to keyhole limpet haemocyanin. These anti‐β3 379–393 antibodies immunoprecipitated in a dose‐dependent manner specific benzodiazepine agonist binding sites from Na+ deoxycholate extracts of bovine cerebral cortex. In immunoblots, anti‐β3 379–393 antibodies recognised two species with M fr 59 900 and M fr 57 200 in all preparations tested, which included crude detergent‐solubilised, benzodiazepine affinity chromatography‐purified receptor, anti‐α1 324–341 antibody, anti‐Cys α2 414–424 antibody and anti‐Cys α3 454–467 antibody immunoaffinity‐purified GABAA‐receptor subpopulations. These results provide evidence for the ubiquity and promiscuity of the GABAA‐receptor β3 subunit.</abstract><cop>Amsterdam</cop><pub>Elsevier</pub><doi>10.1016/0014-5793(91)81390-T</doi><tpages>3</tpages></addata></record>
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issn	0014-5793 1873-3468
language	eng
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source	ScienceDirect®
subjects	Aminoacid receptors (glycine, glutamate, gaba) Antibody Benzodiazepine Biological and medical sciences Cell receptors Cell structures and functions ELISA enzyme linked immunoadsorbent assay Fundamental and applied biological sciences. Psychology GABA GABAA Immunoaffinity keyhole limpet haemocyanin KLH Molecular and cellular biology Purification Receptor SDS-PAGE sodium dodecyl sulphate polyacrylamide gel electrophoresis γ-aminobutyric acid
title	Promiscuity of GABAA‐receptor β3 subunits as demonstrated by their presence in α1, α2 and α3 subunit‐containing receptor subpopulations
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