Assay of γ-glutamyltransferase with amino acid dehydrogenases from Bacillus stearothermophilus as auxiliary enzymes
A spectrophotometric assay for serum γ-glutamyltransferase (γ-GT, EC 2.3.2.2) based on the increasing absorbance at 340 nm due to NADH formation is described. Using γ-glutamyl dipeptides as the donor substrate, amino acids formed by the γ-glutamyl transfer from the donor substrate to the acceptor su...
Gespeichert in:
| Veröffentlicht in: | Clinica chimica acta 1992-04, Vol.207 (1), p.1-9 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 9 |
|---|---|
| container_issue | 1 |
| container_start_page | 1 |
| container_title | Clinica chimica acta |
| container_volume | 207 |
| creator | Kondo, Hitoshi Hashimoto, Mamiko Nagata, Kazuhiko Tomita, Kosuke Tsubota, Hiroyuki |
| description | A spectrophotometric assay for serum γ-glutamyltransferase (γ-GT, EC 2.3.2.2) based on the increasing absorbance at 340 nm due to NADH formation is described. Using γ-glutamyl dipeptides as the donor substrate, amino acids formed by the γ-glutamyl transfer from the donor substrate to the acceptor substrate glycylglycine are stoichiometrically converted by the corresponding amino acid dehydrogenases from
Bacillus stearothermophilus to produce their keto acids and NADH. γ-Glutamylalanine was found to be the most specific and sensitive donor substrate. The method can be mechanized, is free of interference and correlates well with conventional methods. |
| doi_str_mv | 10.1016/0009-8981(92)90145-G |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_72976244</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>000989819290145G</els_id><sourcerecordid>72976244</sourcerecordid><originalsourceid>FETCH-LOGICAL-c301t-7f14fdfdb5f9f36ec65cb62bff30cffd9d5e67d2abb9f74f25ce12c6294d4ed83</originalsourceid><addsrcrecordid>eNp9kMGKFDEQhoMo67j6Bgo5iKyH1iSdTk8uwrroKCx40XNIJ5WdSHdnTHWr7Wvte_hMpp1hvQkFofJ_VRQfIU85e8UZV68ZY7ra6i2_0OKlZlw21e4e2fBtW1e11OI-2dwhD8kjxK-llUzxM3LG64Y1ot6Q6RLRLjQF-vu2uunnyQ5LP2U7YoBsEeiPOO2pHeKYqHXRUw_7xed0A2NJkYacBvq2JH0_I8UJbE7THvKQDvu4ftlS88_YR5sXCuOvZQB8TB4E2yM8Ob3n5Mv7d5-vPlTXn3Yfry6vK1czPlVt4DL44Lsm6FArcKpxnRJdCDVzIXjtG1CtF7brdGhlEI0DLpwSWnoJflufkxfHvYecvs2AkxkiOuh7O0Ka0bRCt0pIWUB5BF1OiBmCOeQ4lIsNZ2aVbVaTZjVptDB_ZZtdGXt22j93A_h_Q0e7JX9-yi0624ei1UW8wxqplOAr9uaIQXHxPUI26CKMDnzM4CbjU_z_HX8AfDygRw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>72976244</pqid></control><display><type>article</type><title>Assay of γ-glutamyltransferase with amino acid dehydrogenases from Bacillus stearothermophilus as auxiliary enzymes</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Kondo, Hitoshi ; Hashimoto, Mamiko ; Nagata, Kazuhiko ; Tomita, Kosuke ; Tsubota, Hiroyuki</creator><creatorcontrib>Kondo, Hitoshi ; Hashimoto, Mamiko ; Nagata, Kazuhiko ; Tomita, Kosuke ; Tsubota, Hiroyuki</creatorcontrib><description>A spectrophotometric assay for serum γ-glutamyltransferase (γ-GT, EC 2.3.2.2) based on the increasing absorbance at 340 nm due to NADH formation is described. Using γ-glutamyl dipeptides as the donor substrate, amino acids formed by the γ-glutamyl transfer from the donor substrate to the acceptor substrate glycylglycine are stoichiometrically converted by the corresponding amino acid dehydrogenases from
Bacillus stearothermophilus to produce their keto acids and NADH. γ-Glutamylalanine was found to be the most specific and sensitive donor substrate. The method can be mechanized, is free of interference and correlates well with conventional methods.</description><identifier>ISSN: 0009-8981</identifier><identifier>EISSN: 1873-3492</identifier><identifier>DOI: 10.1016/0009-8981(92)90145-G</identifier><identifier>PMID: 1350523</identifier><identifier>CODEN: CCATAR</identifier><language>eng</language><publisher>Shannon: Elsevier B.V</publisher><subject>Amino acid dehydrogenase ; Amino Acid Oxidoreductases - metabolism ; Analytical, structural and metabolic biochemistry ; Bacillus stearothermophilus ; Biological and medical sciences ; Dipeptide substrate ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; gamma-Glutamyltransferase - blood ; gamma-Glutamyltransferase - metabolism ; Geobacillus stearothermophilus - enzymology ; Indicators and Reagents - standards ; Spectrophotometric assay ; Spectrophotometry, Ultraviolet ; Transferases ; γ-Glutamyltransferase</subject><ispartof>Clinica chimica acta, 1992-04, Vol.207 (1), p.1-9</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c301t-7f14fdfdb5f9f36ec65cb62bff30cffd9d5e67d2abb9f74f25ce12c6294d4ed83</citedby><cites>FETCH-LOGICAL-c301t-7f14fdfdb5f9f36ec65cb62bff30cffd9d5e67d2abb9f74f25ce12c6294d4ed83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0009-8981(92)90145-G$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5466213$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1350523$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kondo, Hitoshi</creatorcontrib><creatorcontrib>Hashimoto, Mamiko</creatorcontrib><creatorcontrib>Nagata, Kazuhiko</creatorcontrib><creatorcontrib>Tomita, Kosuke</creatorcontrib><creatorcontrib>Tsubota, Hiroyuki</creatorcontrib><title>Assay of γ-glutamyltransferase with amino acid dehydrogenases from Bacillus stearothermophilus as auxiliary enzymes</title><title>Clinica chimica acta</title><addtitle>Clin Chim Acta</addtitle><description>A spectrophotometric assay for serum γ-glutamyltransferase (γ-GT, EC 2.3.2.2) based on the increasing absorbance at 340 nm due to NADH formation is described. Using γ-glutamyl dipeptides as the donor substrate, amino acids formed by the γ-glutamyl transfer from the donor substrate to the acceptor substrate glycylglycine are stoichiometrically converted by the corresponding amino acid dehydrogenases from
Bacillus stearothermophilus to produce their keto acids and NADH. γ-Glutamylalanine was found to be the most specific and sensitive donor substrate. The method can be mechanized, is free of interference and correlates well with conventional methods.</description><subject>Amino acid dehydrogenase</subject><subject>Amino Acid Oxidoreductases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacillus stearothermophilus</subject><subject>Biological and medical sciences</subject><subject>Dipeptide substrate</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gamma-Glutamyltransferase - blood</subject><subject>gamma-Glutamyltransferase - metabolism</subject><subject>Geobacillus stearothermophilus - enzymology</subject><subject>Indicators and Reagents - standards</subject><subject>Spectrophotometric assay</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Transferases</subject><subject>γ-Glutamyltransferase</subject><issn>0009-8981</issn><issn>1873-3492</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMGKFDEQhoMo67j6Bgo5iKyH1iSdTk8uwrroKCx40XNIJ5WdSHdnTHWr7Wvte_hMpp1hvQkFofJ_VRQfIU85e8UZV68ZY7ra6i2_0OKlZlw21e4e2fBtW1e11OI-2dwhD8kjxK-llUzxM3LG64Y1ot6Q6RLRLjQF-vu2uunnyQ5LP2U7YoBsEeiPOO2pHeKYqHXRUw_7xed0A2NJkYacBvq2JH0_I8UJbE7THvKQDvu4ftlS88_YR5sXCuOvZQB8TB4E2yM8Ob3n5Mv7d5-vPlTXn3Yfry6vK1czPlVt4DL44Lsm6FArcKpxnRJdCDVzIXjtG1CtF7brdGhlEI0DLpwSWnoJflufkxfHvYecvs2AkxkiOuh7O0Ka0bRCt0pIWUB5BF1OiBmCOeQ4lIsNZ2aVbVaTZjVptDB_ZZtdGXt22j93A_h_Q0e7JX9-yi0624ei1UW8wxqplOAr9uaIQXHxPUI26CKMDnzM4CbjU_z_HX8AfDygRw</recordid><startdate>19920430</startdate><enddate>19920430</enddate><creator>Kondo, Hitoshi</creator><creator>Hashimoto, Mamiko</creator><creator>Nagata, Kazuhiko</creator><creator>Tomita, Kosuke</creator><creator>Tsubota, Hiroyuki</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><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>19920430</creationdate><title>Assay of γ-glutamyltransferase with amino acid dehydrogenases from Bacillus stearothermophilus as auxiliary enzymes</title><author>Kondo, Hitoshi ; Hashimoto, Mamiko ; Nagata, Kazuhiko ; Tomita, Kosuke ; Tsubota, Hiroyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c301t-7f14fdfdb5f9f36ec65cb62bff30cffd9d5e67d2abb9f74f25ce12c6294d4ed83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino acid dehydrogenase</topic><topic>Amino Acid Oxidoreductases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bacillus stearothermophilus</topic><topic>Biological and medical sciences</topic><topic>Dipeptide substrate</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gamma-Glutamyltransferase - blood</topic><topic>gamma-Glutamyltransferase - metabolism</topic><topic>Geobacillus stearothermophilus - enzymology</topic><topic>Indicators and Reagents - standards</topic><topic>Spectrophotometric assay</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Transferases</topic><topic>γ-Glutamyltransferase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kondo, Hitoshi</creatorcontrib><creatorcontrib>Hashimoto, Mamiko</creatorcontrib><creatorcontrib>Nagata, Kazuhiko</creatorcontrib><creatorcontrib>Tomita, Kosuke</creatorcontrib><creatorcontrib>Tsubota, Hiroyuki</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>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Clinica chimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kondo, Hitoshi</au><au>Hashimoto, Mamiko</au><au>Nagata, Kazuhiko</au><au>Tomita, Kosuke</au><au>Tsubota, Hiroyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Assay of γ-glutamyltransferase with amino acid dehydrogenases from Bacillus stearothermophilus as auxiliary enzymes</atitle><jtitle>Clinica chimica acta</jtitle><addtitle>Clin Chim Acta</addtitle><date>1992-04-30</date><risdate>1992</risdate><volume>207</volume><issue>1</issue><spage>1</spage><epage>9</epage><pages>1-9</pages><issn>0009-8981</issn><eissn>1873-3492</eissn><coden>CCATAR</coden><abstract>A spectrophotometric assay for serum γ-glutamyltransferase (γ-GT, EC 2.3.2.2) based on the increasing absorbance at 340 nm due to NADH formation is described. Using γ-glutamyl dipeptides as the donor substrate, amino acids formed by the γ-glutamyl transfer from the donor substrate to the acceptor substrate glycylglycine are stoichiometrically converted by the corresponding amino acid dehydrogenases from
Bacillus stearothermophilus to produce their keto acids and NADH. γ-Glutamylalanine was found to be the most specific and sensitive donor substrate. The method can be mechanized, is free of interference and correlates well with conventional methods.</abstract><cop>Shannon</cop><pub>Elsevier B.V</pub><pmid>1350523</pmid><doi>10.1016/0009-8981(92)90145-G</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0009-8981 |
| ispartof | Clinica chimica acta, 1992-04, Vol.207 (1), p.1-9 |
| issn | 0009-8981 1873-3492 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72976244 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino acid dehydrogenase Amino Acid Oxidoreductases - metabolism Analytical, structural and metabolic biochemistry Bacillus stearothermophilus Biological and medical sciences Dipeptide substrate Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology gamma-Glutamyltransferase - blood gamma-Glutamyltransferase - metabolism Geobacillus stearothermophilus - enzymology Indicators and Reagents - standards Spectrophotometric assay Spectrophotometry, Ultraviolet Transferases γ-Glutamyltransferase |
| title | Assay of γ-glutamyltransferase with amino acid dehydrogenases from Bacillus stearothermophilus as auxiliary enzymes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T22%3A21%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Assay%20of%20%CE%B3-glutamyltransferase%20with%20amino%20acid%20dehydrogenases%20from%20Bacillus%20stearothermophilus%20as%20auxiliary%20enzymes&rft.jtitle=Clinica%20chimica%20acta&rft.au=Kondo,%20Hitoshi&rft.date=1992-04-30&rft.volume=207&rft.issue=1&rft.spage=1&rft.epage=9&rft.pages=1-9&rft.issn=0009-8981&rft.eissn=1873-3492&rft.coden=CCATAR&rft_id=info:doi/10.1016/0009-8981(92)90145-G&rft_dat=%3Cproquest_cross%3E72976244%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=72976244&rft_id=info:pmid/1350523&rft_els_id=000989819290145G&rfr_iscdi=true |