[50] γ-Glutamyl transpeptidase from kidney
This chapter focuses on mammalian γ-glutamyl transpeptidase, emphasizing the rat kidney enzyme, the most extensively studied transpeptidase. γ-glutamyl transpeptidase plays a key role in the γ-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. Glutathione is synthesized from...
Gespeichert in:
| Veröffentlicht in: | Methods in Enzymology 1985, Vol.113, p.400-419 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 419 |
|---|---|
| container_issue | |
| container_start_page | 400 |
| container_title | Methods in Enzymology |
| container_volume | 113 |
| creator | Tate, Suresh S. Meister, Alton |
| description | This chapter focuses on mammalian γ-glutamyl transpeptidase, emphasizing the rat kidney enzyme, the most extensively studied transpeptidase. γ-glutamyl transpeptidase plays a key role in the γ-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. Glutathione is synthesized from its constituent amino acids within the cells by the successive actions of γ-glutamylcysteine and glutathione synthetases. The reactions allow the storage of cysteine as glutathione and γ-glutamyl transpeptidase catalyzes the first step in the pathway that leads to release of the cysteine moiety from the tripeptide. Homogenates of animal tissues exhibit a wide range of transpeptidase activity. Low transpeptidase activity in a tissue homogenate is often misleading because specific localization studies indicate that there are specific regions of intense enzyme activity in many tissues. In most mammals, the kidney exhibits by far the highest activity. |
| doi_str_mv | 10.1016/S0076-6879(85)13053-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_76588317</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0076687985130533</els_id><sourcerecordid>76588317</sourcerecordid><originalsourceid>FETCH-LOGICAL-c229t-47e3084e57a8f6d60fd3683e4365719dd63bd74cece16dee5b863c6bbd3103543</originalsourceid><addsrcrecordid>eNo9kN1Kw0AQhRd_qLX2EQq5EkWiu5ns7uRKpGgVCl6oVyJLsjuBaH5qNhH6XL6Hz2Rai1dzcc7MmfMxNhP8UnChrp441ypUqJMzlOcCuIQQ9thYSKlDnSDus2mikYtIYMQF4AEb_68csWPv3zmPNCZixEYRKoSEj9nFq-Rvwc93uCj7Lq3WZdC1ae1XtOoKl3oK8rapgo_C1bQ-YYd5Wnqa7uaEvdzdPs_vw-Xj4mF-swxtFCVdGGsCjjFJnWKunOK5gyGNYlBSi8Q5BZnTsSVLQjkimaECq7LMgeAgY5iw07-7q7b57Ml3piq8pbJMa2p6b7SSiCD0YJztjH1WkTOrtqjSdm127Qb9-k-n4duvglrjbUG1JVe0ZDvjmsIIbjZ4zRav2bAyKM0WrwH4BTZJaIc</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76588317</pqid></control><display><type>article</type><title>[50] γ-Glutamyl transpeptidase from kidney</title><source>MEDLINE</source><source>ScienceDirect eBooks</source><source>Access via ScienceDirect (Elsevier)</source><creator>Tate, Suresh S. ; Meister, Alton</creator><creatorcontrib>Tate, Suresh S. ; Meister, Alton</creatorcontrib><description>This chapter focuses on mammalian γ-glutamyl transpeptidase, emphasizing the rat kidney enzyme, the most extensively studied transpeptidase. γ-glutamyl transpeptidase plays a key role in the γ-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. Glutathione is synthesized from its constituent amino acids within the cells by the successive actions of γ-glutamylcysteine and glutathione synthetases. The reactions allow the storage of cysteine as glutathione and γ-glutamyl transpeptidase catalyzes the first step in the pathway that leads to release of the cysteine moiety from the tripeptide. Homogenates of animal tissues exhibit a wide range of transpeptidase activity. Low transpeptidase activity in a tissue homogenate is often misleading because specific localization studies indicate that there are specific regions of intense enzyme activity in many tissues. In most mammals, the kidney exhibits by far the highest activity.</description><identifier>ISSN: 0076-6879</identifier><identifier>ISBN: 9780121820138</identifier><identifier>ISBN: 0121820130</identifier><identifier>EISSN: 1557-7988</identifier><identifier>DOI: 10.1016/S0076-6879(85)13053-3</identifier><identifier>PMID: 2868390</identifier><language>eng</language><publisher>United States: Elsevier Science & Technology</publisher><subject>Animals ; Antibodies ; Chromatography, Affinity - methods ; gamma-Glutamyltransferase - biosynthesis ; gamma-Glutamyltransferase - isolation & purification ; gamma-Glutamyltransferase - metabolism ; Indicators and Reagents ; Kidney - enzymology ; Kinetics ; Macromolecular Substances ; Male ; Microvilli - enzymology ; Molecular Weight ; Rats ; Rats, Inbred Strains ; Spectrophotometry - methods</subject><ispartof>Methods in Enzymology, 1985, Vol.113, p.400-419</ispartof><rights>1985</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c229t-47e3084e57a8f6d60fd3683e4365719dd63bd74cece16dee5b863c6bbd3103543</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0076687985130533$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,779,780,784,793,3459,3550,4024,11288,27923,27924,27925,45810,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2868390$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tate, Suresh S.</creatorcontrib><creatorcontrib>Meister, Alton</creatorcontrib><title>[50] γ-Glutamyl transpeptidase from kidney</title><title>Methods in Enzymology</title><addtitle>Methods Enzymol</addtitle><description>This chapter focuses on mammalian γ-glutamyl transpeptidase, emphasizing the rat kidney enzyme, the most extensively studied transpeptidase. γ-glutamyl transpeptidase plays a key role in the γ-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. Glutathione is synthesized from its constituent amino acids within the cells by the successive actions of γ-glutamylcysteine and glutathione synthetases. The reactions allow the storage of cysteine as glutathione and γ-glutamyl transpeptidase catalyzes the first step in the pathway that leads to release of the cysteine moiety from the tripeptide. Homogenates of animal tissues exhibit a wide range of transpeptidase activity. Low transpeptidase activity in a tissue homogenate is often misleading because specific localization studies indicate that there are specific regions of intense enzyme activity in many tissues. In most mammals, the kidney exhibits by far the highest activity.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Chromatography, Affinity - methods</subject><subject>gamma-Glutamyltransferase - biosynthesis</subject><subject>gamma-Glutamyltransferase - isolation & purification</subject><subject>gamma-Glutamyltransferase - metabolism</subject><subject>Indicators and Reagents</subject><subject>Kidney - enzymology</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Male</subject><subject>Microvilli - enzymology</subject><subject>Molecular Weight</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Spectrophotometry - methods</subject><issn>0076-6879</issn><issn>1557-7988</issn><isbn>9780121820138</isbn><isbn>0121820130</isbn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kN1Kw0AQhRd_qLX2EQq5EkWiu5ns7uRKpGgVCl6oVyJLsjuBaH5qNhH6XL6Hz2Rai1dzcc7MmfMxNhP8UnChrp441ypUqJMzlOcCuIQQ9thYSKlDnSDus2mikYtIYMQF4AEb_68csWPv3zmPNCZixEYRKoSEj9nFq-Rvwc93uCj7Lq3WZdC1ae1XtOoKl3oK8rapgo_C1bQ-YYd5Wnqa7uaEvdzdPs_vw-Xj4mF-swxtFCVdGGsCjjFJnWKunOK5gyGNYlBSi8Q5BZnTsSVLQjkimaECq7LMgeAgY5iw07-7q7b57Ml3piq8pbJMa2p6b7SSiCD0YJztjH1WkTOrtqjSdm127Qb9-k-n4duvglrjbUG1JVe0ZDvjmsIIbjZ4zRav2bAyKM0WrwH4BTZJaIc</recordid><startdate>1985</startdate><enddate>1985</enddate><creator>Tate, Suresh S.</creator><creator>Meister, Alton</creator><general>Elsevier Science & Technology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>1985</creationdate><title>[50] γ-Glutamyl transpeptidase from kidney</title><author>Tate, Suresh S. ; Meister, Alton</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c229t-47e3084e57a8f6d60fd3683e4365719dd63bd74cece16dee5b863c6bbd3103543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Chromatography, Affinity - methods</topic><topic>gamma-Glutamyltransferase - biosynthesis</topic><topic>gamma-Glutamyltransferase - isolation & purification</topic><topic>gamma-Glutamyltransferase - metabolism</topic><topic>Indicators and Reagents</topic><topic>Kidney - enzymology</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Male</topic><topic>Microvilli - enzymology</topic><topic>Molecular Weight</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Spectrophotometry - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tate, Suresh S.</creatorcontrib><creatorcontrib>Meister, Alton</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Methods in Enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tate, Suresh S.</au><au>Meister, Alton</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>[50] γ-Glutamyl transpeptidase from kidney</atitle><jtitle>Methods in Enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>1985</date><risdate>1985</risdate><volume>113</volume><spage>400</spage><epage>419</epage><pages>400-419</pages><issn>0076-6879</issn><eissn>1557-7988</eissn><isbn>9780121820138</isbn><isbn>0121820130</isbn><abstract>This chapter focuses on mammalian γ-glutamyl transpeptidase, emphasizing the rat kidney enzyme, the most extensively studied transpeptidase. γ-glutamyl transpeptidase plays a key role in the γ-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. Glutathione is synthesized from its constituent amino acids within the cells by the successive actions of γ-glutamylcysteine and glutathione synthetases. The reactions allow the storage of cysteine as glutathione and γ-glutamyl transpeptidase catalyzes the first step in the pathway that leads to release of the cysteine moiety from the tripeptide. Homogenates of animal tissues exhibit a wide range of transpeptidase activity. Low transpeptidase activity in a tissue homogenate is often misleading because specific localization studies indicate that there are specific regions of intense enzyme activity in many tissues. In most mammals, the kidney exhibits by far the highest activity.</abstract><cop>United States</cop><pub>Elsevier Science & Technology</pub><pmid>2868390</pmid><doi>10.1016/S0076-6879(85)13053-3</doi><tpages>20</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0076-6879 |
| ispartof | Methods in Enzymology, 1985, Vol.113, p.400-419 |
| issn | 0076-6879 1557-7988 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76588317 |
| source | MEDLINE; ScienceDirect eBooks; Access via ScienceDirect (Elsevier) |
| subjects | Animals Antibodies Chromatography, Affinity - methods gamma-Glutamyltransferase - biosynthesis gamma-Glutamyltransferase - isolation & purification gamma-Glutamyltransferase - metabolism Indicators and Reagents Kidney - enzymology Kinetics Macromolecular Substances Male Microvilli - enzymology Molecular Weight Rats Rats, Inbred Strains Spectrophotometry - methods |
| title | [50] γ-Glutamyl transpeptidase from kidney |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-21T15%3A22%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=%5B50%5D%20%CE%B3-Glutamyl%20transpeptidase%20from%20kidney&rft.jtitle=Methods%20in%20Enzymology&rft.au=Tate,%20Suresh%20S.&rft.date=1985&rft.volume=113&rft.spage=400&rft.epage=419&rft.pages=400-419&rft.issn=0076-6879&rft.eissn=1557-7988&rft.isbn=9780121820138&rft.isbn_list=0121820130&rft_id=info:doi/10.1016/S0076-6879(85)13053-3&rft_dat=%3Cproquest_pubme%3E76588317%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76588317&rft_id=info:pmid/2868390&rft_els_id=S0076687985130533&rfr_iscdi=true |