Distribution and tissue specificity of 4-aminobutyrate-2-oxoglutarate aminotransferase
A rapid and specific method for assaying 4-aminobutyrate-2-oxoglutarate aminotransferase was developed. The method was based on the selectivity of ion exchange resin and the speed of vacuum filtration. With this new method, the aminotransferase activity in various tissues has been determined as foll...
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Veröffentlicht in: | Neurochemical research 1978-04, Vol.3 (2), p.207-219 |
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description | A rapid and specific method for assaying 4-aminobutyrate-2-oxoglutarate aminotransferase was developed. The method was based on the selectivity of ion exchange resin and the speed of vacuum filtration. With this new method, the aminotransferase activity in various tissues has been determined as follows: brain, 10.2; spinal cord, 11.8; liver, 5.7; kidney, 4.6; heart, 0.5; lung, 0.4 nmol glutamate formed/min/mg. No activity could be detected in muscle preparations. When the aminotransferases were tested with the antibody against the purified 4-aminobutyrate aminotransferase from brain, no difference could be detected among brain, spinal cord, and kidney preparations as judged from the results of immunodiffusion, inhibition of enzyme activity by antibody, and microcomplement fixation. It is concluded that 4-aminobutyrate aminotransferases from various tissues of the mouse are probably identical or closely related. |
doi_str_mv | 10.1007/bf00964061 |
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The method was based on the selectivity of ion exchange resin and the speed of vacuum filtration. With this new method, the aminotransferase activity in various tissues has been determined as follows: brain, 10.2; spinal cord, 11.8; liver, 5.7; kidney, 4.6; heart, 0.5; lung, 0.4 nmol glutamate formed/min/mg. No activity could be detected in muscle preparations. When the aminotransferases were tested with the antibody against the purified 4-aminobutyrate aminotransferase from brain, no difference could be detected among brain, spinal cord, and kidney preparations as judged from the results of immunodiffusion, inhibition of enzyme activity by antibody, and microcomplement fixation. It is concluded that 4-aminobutyrate aminotransferases from various tissues of the mouse are probably identical or closely related.</description><identifier>ISSN: 0364-3190</identifier><identifier>EISSN: 1573-6903</identifier><identifier>DOI: 10.1007/bf00964061</identifier><identifier>PMID: 97570</identifier><language>eng</language><publisher>United States</publisher><subject>4-Aminobutyrate Transaminase - analysis ; Animals ; Brain - enzymology ; Carbon Radioisotopes ; Complement Fixation Tests ; Immunodiffusion ; Isotope Labeling - methods ; Kinetics ; Mice ; Spinal Cord - enzymology ; Tissue Distribution ; Transaminases - analysis</subject><ispartof>Neurochemical research, 1978-04, Vol.3 (2), p.207-219</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-4859cce32d13799521bfb6dc383b05f74abcf341ac58984a7709b9caa4c16bb23</citedby><cites>FETCH-LOGICAL-c375t-4859cce32d13799521bfb6dc383b05f74abcf341ac58984a7709b9caa4c16bb23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/97570$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, J Y</creatorcontrib><creatorcontrib>Moss, L G</creatorcontrib><creatorcontrib>Chude, O</creatorcontrib><title>Distribution and tissue specificity of 4-aminobutyrate-2-oxoglutarate aminotransferase</title><title>Neurochemical research</title><addtitle>Neurochem Res</addtitle><description>A rapid and specific method for assaying 4-aminobutyrate-2-oxoglutarate aminotransferase was developed. The method was based on the selectivity of ion exchange resin and the speed of vacuum filtration. With this new method, the aminotransferase activity in various tissues has been determined as follows: brain, 10.2; spinal cord, 11.8; liver, 5.7; kidney, 4.6; heart, 0.5; lung, 0.4 nmol glutamate formed/min/mg. No activity could be detected in muscle preparations. When the aminotransferases were tested with the antibody against the purified 4-aminobutyrate aminotransferase from brain, no difference could be detected among brain, spinal cord, and kidney preparations as judged from the results of immunodiffusion, inhibition of enzyme activity by antibody, and microcomplement fixation. It is concluded that 4-aminobutyrate aminotransferases from various tissues of the mouse are probably identical or closely related.</description><subject>4-Aminobutyrate Transaminase - analysis</subject><subject>Animals</subject><subject>Brain - enzymology</subject><subject>Carbon Radioisotopes</subject><subject>Complement Fixation Tests</subject><subject>Immunodiffusion</subject><subject>Isotope Labeling - methods</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Spinal Cord - enzymology</subject><subject>Tissue Distribution</subject><subject>Transaminases - analysis</subject><issn>0364-3190</issn><issn>1573-6903</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo90DFPwzAQBWALUUEpLKwsmRiQDOfYjusRCgWkSizAGtmOjYySuNiORP89oS1Mp6f79IaH0DmBawIgbrQDkBWDihygKeGC4koCPURToBXDlEg4RicpfQKMvCRHaCIFFzBF7_c-5ej1kH3oC9U3RfYpDbZIa2u888bnTRFcwbDqfB9Gt4kqW1zi8B0-2iGr31hsnzmqPjkbVbKnaOJUm-zZ_s7Q2_LhdfGEVy-Pz4vbFTZU8IzZnEtjLC0bQoWUvCTa6aoxdE41cCeY0sZRRpThczlnSgiQWhqlmCGV1iWdoctd7zqGr8GmXHc-Gdu2qrdhSLVgICgDPsKrHTQxpBStq9fRdypuagL174T13fJvwhFf7FsH3dnmn243oz92m2y3</recordid><startdate>197804</startdate><enddate>197804</enddate><creator>Wu, J Y</creator><creator>Moss, L G</creator><creator>Chude, O</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>197804</creationdate><title>Distribution and tissue specificity of 4-aminobutyrate-2-oxoglutarate aminotransferase</title><author>Wu, J Y ; Moss, L G ; Chude, O</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-4859cce32d13799521bfb6dc383b05f74abcf341ac58984a7709b9caa4c16bb23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>4-Aminobutyrate Transaminase - analysis</topic><topic>Animals</topic><topic>Brain - enzymology</topic><topic>Carbon Radioisotopes</topic><topic>Complement Fixation Tests</topic><topic>Immunodiffusion</topic><topic>Isotope Labeling - methods</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Spinal Cord - enzymology</topic><topic>Tissue Distribution</topic><topic>Transaminases - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, J Y</creatorcontrib><creatorcontrib>Moss, L G</creatorcontrib><creatorcontrib>Chude, O</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Neurochemical research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, J Y</au><au>Moss, L G</au><au>Chude, O</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distribution and tissue specificity of 4-aminobutyrate-2-oxoglutarate aminotransferase</atitle><jtitle>Neurochemical research</jtitle><addtitle>Neurochem Res</addtitle><date>1978-04</date><risdate>1978</risdate><volume>3</volume><issue>2</issue><spage>207</spage><epage>219</epage><pages>207-219</pages><issn>0364-3190</issn><eissn>1573-6903</eissn><abstract>A rapid and specific method for assaying 4-aminobutyrate-2-oxoglutarate aminotransferase was developed. The method was based on the selectivity of ion exchange resin and the speed of vacuum filtration. With this new method, the aminotransferase activity in various tissues has been determined as follows: brain, 10.2; spinal cord, 11.8; liver, 5.7; kidney, 4.6; heart, 0.5; lung, 0.4 nmol glutamate formed/min/mg. No activity could be detected in muscle preparations. When the aminotransferases were tested with the antibody against the purified 4-aminobutyrate aminotransferase from brain, no difference could be detected among brain, spinal cord, and kidney preparations as judged from the results of immunodiffusion, inhibition of enzyme activity by antibody, and microcomplement fixation. It is concluded that 4-aminobutyrate aminotransferases from various tissues of the mouse are probably identical or closely related.</abstract><cop>United States</cop><pmid>97570</pmid><doi>10.1007/bf00964061</doi><tpages>13</tpages></addata></record> |
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subjects | 4-Aminobutyrate Transaminase - analysis Animals Brain - enzymology Carbon Radioisotopes Complement Fixation Tests Immunodiffusion Isotope Labeling - methods Kinetics Mice Spinal Cord - enzymology Tissue Distribution Transaminases - analysis |
title | Distribution and tissue specificity of 4-aminobutyrate-2-oxoglutarate aminotransferase |
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