Biochemical characterization of kainate receptors from goldfish brain
Kainate receptors from goldfish brain were purified by affinity chromatography. Unlike previously published purifications, which have yielded single proteins of 48-50 kDa from frog, chick, and pigeon brain, our preparations contained two polypeptides, of 41 kDa and 45 kDa. In addition, a broad band...
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| Veröffentlicht in: | Molecular pharmacology 1992-08, Vol.42 (2), p.203-209 |
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| creator | ZIEGRA, C. J WILLARD, J. M OSWALD, R. E |
| description | Kainate receptors from goldfish brain were purified by affinity chromatography. Unlike previously published purifications,
which have yielded single proteins of 48-50 kDa from frog, chick, and pigeon brain, our preparations contained two polypeptides,
of 41 kDa and 45 kDa. In addition, a broad band centered at 120 kDa was present. Some of the 41-kDa and 45-kDa polypeptides
were derived from the higher molecular mass protein. All of these proteins were recognized by a monoclonal antibody produced
against a purified frog kainate receptor. The distribution of the 41-kDa and 45-kDa proteins varied independently in different
major brain regions, suggesting that they can exist as separate independent proteins. A partial amino acid sequence of the
41-kDa polypeptide is very similar (40-60% identity) to specific segments of the frog and chick kainate-binding proteins and
the alpha-amino-3-hydroxy-5-methylisoxazolepropionate/kainate ion channels. The characteristics of the 41-kDa and 45-kDa polypeptides
suggest that these two proteins are distinct. Photo-affinity labeling with [3H]kainate showed that a [3H]kainate binding site
is associated with the 41-kDa polypeptide, and peptide mapping suggests that the two proteins are not identical. In addition,
the two peptides do not appear to be related by differential glycosylation or phosphorylation. The 41-kDa and 45-kDa polypeptides,
therefore, appear to be distinct and may represent kainate receptor subtypes or, in some cases, possibly two different subunits
of a kainate receptor complex. |
| format | Article |
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which have yielded single proteins of 48-50 kDa from frog, chick, and pigeon brain, our preparations contained two polypeptides,
of 41 kDa and 45 kDa. In addition, a broad band centered at 120 kDa was present. Some of the 41-kDa and 45-kDa polypeptides
were derived from the higher molecular mass protein. All of these proteins were recognized by a monoclonal antibody produced
against a purified frog kainate receptor. The distribution of the 41-kDa and 45-kDa proteins varied independently in different
major brain regions, suggesting that they can exist as separate independent proteins. A partial amino acid sequence of the
41-kDa polypeptide is very similar (40-60% identity) to specific segments of the frog and chick kainate-binding proteins and
the alpha-amino-3-hydroxy-5-methylisoxazolepropionate/kainate ion channels. The characteristics of the 41-kDa and 45-kDa polypeptides
suggest that these two proteins are distinct. Photo-affinity labeling with [3H]kainate showed that a [3H]kainate binding site
is associated with the 41-kDa polypeptide, and peptide mapping suggests that the two proteins are not identical. In addition,
the two peptides do not appear to be related by differential glycosylation or phosphorylation. The 41-kDa and 45-kDa polypeptides,
therefore, appear to be distinct and may represent kainate receptor subtypes or, in some cases, possibly two different subunits
of a kainate receptor complex.</description><identifier>ISSN: 0026-895X</identifier><identifier>EISSN: 1521-0111</identifier><identifier>PMID: 1381042</identifier><identifier>CODEN: MOPMA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Pharmacology and Experimental Therapeutics</publisher><subject>affinity chromatography ; Amino Acid Sequence ; Aminoacid receptors (glycine, glutamate, gaba) ; Animals ; Anura ; biochemistry ; Biological and medical sciences ; brain ; Brain - ultrastructure ; Carassius auratus ; Cell receptors ; Cell structures and functions ; Chromatography, Affinity ; Electrophoresis, Polyacrylamide Gel ; Epitopes - analysis ; Freshwater ; Fundamental and applied biological sciences. Psychology ; Goldfish - metabolism ; kainic acid ; Kainic Acid - metabolism ; Membranes - ultrastructure ; Molecular and cellular biology ; Molecular Sequence Data ; Nerve Tissue Proteins - analysis ; Nerve Tissue Proteins - metabolism ; purification ; receptors ; Receptors, Kainic Acid ; Receptors, Neurotransmitter - isolation & purification ; Receptors, Neurotransmitter - metabolism ; Sequence Homology, Nucleic Acid ; Sodium Dodecyl Sulfate ; Synapses - ultrastructure ; Tritium</subject><ispartof>Molecular pharmacology, 1992-08, Vol.42 (2), p.203-209</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4398539$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1381042$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ZIEGRA, C. J</creatorcontrib><creatorcontrib>WILLARD, J. M</creatorcontrib><creatorcontrib>OSWALD, R. E</creatorcontrib><title>Biochemical characterization of kainate receptors from goldfish brain</title><title>Molecular pharmacology</title><addtitle>Mol Pharmacol</addtitle><description>Kainate receptors from goldfish brain were purified by affinity chromatography. Unlike previously published purifications,
which have yielded single proteins of 48-50 kDa from frog, chick, and pigeon brain, our preparations contained two polypeptides,
of 41 kDa and 45 kDa. In addition, a broad band centered at 120 kDa was present. Some of the 41-kDa and 45-kDa polypeptides
were derived from the higher molecular mass protein. All of these proteins were recognized by a monoclonal antibody produced
against a purified frog kainate receptor. The distribution of the 41-kDa and 45-kDa proteins varied independently in different
major brain regions, suggesting that they can exist as separate independent proteins. A partial amino acid sequence of the
41-kDa polypeptide is very similar (40-60% identity) to specific segments of the frog and chick kainate-binding proteins and
the alpha-amino-3-hydroxy-5-methylisoxazolepropionate/kainate ion channels. The characteristics of the 41-kDa and 45-kDa polypeptides
suggest that these two proteins are distinct. Photo-affinity labeling with [3H]kainate showed that a [3H]kainate binding site
is associated with the 41-kDa polypeptide, and peptide mapping suggests that the two proteins are not identical. In addition,
the two peptides do not appear to be related by differential glycosylation or phosphorylation. The 41-kDa and 45-kDa polypeptides,
therefore, appear to be distinct and may represent kainate receptor subtypes or, in some cases, possibly two different subunits
of a kainate receptor complex.</description><subject>affinity chromatography</subject><subject>Amino Acid Sequence</subject><subject>Aminoacid receptors (glycine, glutamate, gaba)</subject><subject>Animals</subject><subject>Anura</subject><subject>biochemistry</subject><subject>Biological and medical sciences</subject><subject>brain</subject><subject>Brain - ultrastructure</subject><subject>Carassius auratus</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Chromatography, Affinity</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Epitopes - analysis</subject><subject>Freshwater</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Goldfish - metabolism</subject><subject>kainic acid</subject><subject>Kainic Acid - metabolism</subject><subject>Membranes - ultrastructure</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - analysis</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>purification</subject><subject>receptors</subject><subject>Receptors, Kainic Acid</subject><subject>Receptors, Neurotransmitter - isolation & purification</subject><subject>Receptors, Neurotransmitter - metabolism</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Sodium Dodecyl Sulfate</subject><subject>Synapses - ultrastructure</subject><subject>Tritium</subject><issn>0026-895X</issn><issn>1521-0111</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE9LwzAYh4Moc04_gtCDeivkb5ccdWwqDLwoeCtp-maNtk1NOkQ_vZEVr_Ie3sPv4Tk8R2hOBCU5JoQcoznGtMilEq-n6CzGN4wJFxLP0IwwSTCnc7S-c9400Dmj28w0OmgzQnDfenS-z7zN3rXr9QhZAAPD6EPMbPBdtvNtbV1ssiok4BydWN1GuJj-Ar1s1s-rh3z7dP-4ut3mDVXFmFsudM0E4wWV3EhLMcaFAlorIllNJFdEiFosBTBmuOTCVJgzqCwIaQtL2QLdHLxD8B97iGPZuWigbXUPfh_LJUuCIsn-A0nB8ZIrlcDLCdxXHdTlEFynw1c5BUr71bTrmBLZoHvj4h_GmZKC_WquD1jjds2nC1AOqWWnjW_9LmG0TIcZ-wH8untk</recordid><startdate>19920801</startdate><enddate>19920801</enddate><creator>ZIEGRA, C. 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E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h296t-f45ad35346284c8f200069e2d9183d1849155d575e33c4845cb043ebfe58f6f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>affinity chromatography</topic><topic>Amino Acid Sequence</topic><topic>Aminoacid receptors (glycine, glutamate, gaba)</topic><topic>Animals</topic><topic>Anura</topic><topic>biochemistry</topic><topic>Biological and medical sciences</topic><topic>brain</topic><topic>Brain - ultrastructure</topic><topic>Carassius auratus</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Chromatography, Affinity</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Epitopes - analysis</topic><topic>Freshwater</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Goldfish - metabolism</topic><topic>kainic acid</topic><topic>Kainic Acid - metabolism</topic><topic>Membranes - ultrastructure</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - analysis</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>purification</topic><topic>receptors</topic><topic>Receptors, Kainic Acid</topic><topic>Receptors, Neurotransmitter - isolation & purification</topic><topic>Receptors, Neurotransmitter - metabolism</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Sodium Dodecyl Sulfate</topic><topic>Synapses - ultrastructure</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ZIEGRA, C. J</creatorcontrib><creatorcontrib>WILLARD, J. M</creatorcontrib><creatorcontrib>OSWALD, R. E</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biochemistry Abstracts 1</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ZIEGRA, C. J</au><au>WILLARD, J. M</au><au>OSWALD, R. E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical characterization of kainate receptors from goldfish brain</atitle><jtitle>Molecular pharmacology</jtitle><addtitle>Mol Pharmacol</addtitle><date>1992-08-01</date><risdate>1992</risdate><volume>42</volume><issue>2</issue><spage>203</spage><epage>209</epage><pages>203-209</pages><issn>0026-895X</issn><eissn>1521-0111</eissn><coden>MOPMA3</coden><abstract>Kainate receptors from goldfish brain were purified by affinity chromatography. Unlike previously published purifications,
which have yielded single proteins of 48-50 kDa from frog, chick, and pigeon brain, our preparations contained two polypeptides,
of 41 kDa and 45 kDa. In addition, a broad band centered at 120 kDa was present. Some of the 41-kDa and 45-kDa polypeptides
were derived from the higher molecular mass protein. All of these proteins were recognized by a monoclonal antibody produced
against a purified frog kainate receptor. The distribution of the 41-kDa and 45-kDa proteins varied independently in different
major brain regions, suggesting that they can exist as separate independent proteins. A partial amino acid sequence of the
41-kDa polypeptide is very similar (40-60% identity) to specific segments of the frog and chick kainate-binding proteins and
the alpha-amino-3-hydroxy-5-methylisoxazolepropionate/kainate ion channels. The characteristics of the 41-kDa and 45-kDa polypeptides
suggest that these two proteins are distinct. Photo-affinity labeling with [3H]kainate showed that a [3H]kainate binding site
is associated with the 41-kDa polypeptide, and peptide mapping suggests that the two proteins are not identical. In addition,
the two peptides do not appear to be related by differential glycosylation or phosphorylation. The 41-kDa and 45-kDa polypeptides,
therefore, appear to be distinct and may represent kainate receptor subtypes or, in some cases, possibly two different subunits
of a kainate receptor complex.</abstract><cop>Bethesda, MD</cop><pub>American Society for Pharmacology and Experimental Therapeutics</pub><pmid>1381042</pmid><tpages>7</tpages></addata></record> |
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| ispartof | Molecular pharmacology, 1992-08, Vol.42 (2), p.203-209 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | affinity chromatography Amino Acid Sequence Aminoacid receptors (glycine, glutamate, gaba) Animals Anura biochemistry Biological and medical sciences brain Brain - ultrastructure Carassius auratus Cell receptors Cell structures and functions Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Epitopes - analysis Freshwater Fundamental and applied biological sciences. Psychology Goldfish - metabolism kainic acid Kainic Acid - metabolism Membranes - ultrastructure Molecular and cellular biology Molecular Sequence Data Nerve Tissue Proteins - analysis Nerve Tissue Proteins - metabolism purification receptors Receptors, Kainic Acid Receptors, Neurotransmitter - isolation & purification Receptors, Neurotransmitter - metabolism Sequence Homology, Nucleic Acid Sodium Dodecyl Sulfate Synapses - ultrastructure Tritium |
| title | Biochemical characterization of kainate receptors from goldfish brain |
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