Increased liver L-serine-pyruvate aminotransferase activity under gluconeogenic conditions
Rat liver l-serine-pyruvate aminotransferase activity exceeds markedly the normal adult value (a) in the neonatal period, (b) after glucagon injection and (c) after alloxan injection, observations that reinforce the suggestion from comparative findings that the aminotransferase has a role in glucone...
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| Veröffentlicht in: | Biochemical journal 1973-05, Vol.134 (1), p.349-351 |
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| creator | Rowsell, E V al-Tai, A H Carnie, J A |
| description | Rat liver l-serine-pyruvate aminotransferase activity exceeds markedly the normal adult value (a) in the neonatal period, (b) after glucagon injection and (c) after alloxan injection, observations that reinforce the suggestion from comparative findings that the aminotransferase has a role in gluconeogenesis. Some findings, however, argue in favour of l-serine dehydratase as the enzyme of gluconeogenesis from l-serine. |
| doi_str_mv | 10.1042/bj1340349 |
| format | Article |
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Some findings, however, argue in favour of l-serine dehydratase as the enzyme of gluconeogenesis from l-serine.</description><identifier>ISSN: 0264-6021</identifier><identifier>ISSN: 0306-3283</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj1340349</identifier><identifier>PMID: 4723229</identifier><language>eng</language><publisher>England</publisher><subject>Aging ; Alloxan - pharmacology ; Animals ; Animals, Newborn ; Development ; Female ; Fetus ; Glucagon - pharmacology ; Gluconeogenesis ; L-Serine Dehydratase - metabolism ; Liver - drug effects ; Liver - enzymology ; Liver - growth & development ; Pregnancy ; Pyruvates ; Rats ; Serine ; Transaminases - metabolism</subject><ispartof>Biochemical journal, 1973-05, Vol.134 (1), p.349-351</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c436t-77c4871f626482727474ed29eb17c02eb5d56667203b43d09ff6db2bf218f8c83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1177815/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1177815/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4723229$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rowsell, E V</creatorcontrib><creatorcontrib>al-Tai, A H</creatorcontrib><creatorcontrib>Carnie, J A</creatorcontrib><title>Increased liver L-serine-pyruvate aminotransferase activity under gluconeogenic conditions</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Rat liver l-serine-pyruvate aminotransferase activity exceeds markedly the normal adult value (a) in the neonatal period, (b) after glucagon injection and (c) after alloxan injection, observations that reinforce the suggestion from comparative findings that the aminotransferase has a role in gluconeogenesis. Some findings, however, argue in favour of l-serine dehydratase as the enzyme of gluconeogenesis from l-serine.</description><subject>Aging</subject><subject>Alloxan - pharmacology</subject><subject>Animals</subject><subject>Animals, Newborn</subject><subject>Development</subject><subject>Female</subject><subject>Fetus</subject><subject>Glucagon - pharmacology</subject><subject>Gluconeogenesis</subject><subject>L-Serine Dehydratase - metabolism</subject><subject>Liver - drug effects</subject><subject>Liver - enzymology</subject><subject>Liver - growth & development</subject><subject>Pregnancy</subject><subject>Pyruvates</subject><subject>Rats</subject><subject>Serine</subject><subject>Transaminases - metabolism</subject><issn>0264-6021</issn><issn>0306-3283</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU1LAzEQhoMotVYP_gBhT4KH1Xw1yV4EKX4UCl704iVks7M1ZTdbk92F_nsjlqKnGZhn3nlnBqFLgm8J5vSu3BDGMePFEZoSLnGuJFXHaIqp4LnAlJyisxg3GBOOOZ6gCZeUUVpM0cfS2wAmQpU1boSQrfIIwXnIt7swjKaHzLTOd30wPtYQEpkZ27vR9bts8FXqWDeD7Tx0a_DOZimtXO86H8_RSW2aCBf7OEPvT49vi5d89fq8XDyscsuZ6HMpLVeS1CJ5VVRSySWHihZQEmkxhXJezYUQkmJWclbhoq5FVdKypkTVyio2Q_e_utuhbKGy4JPZRm-Da03Y6c44_b_i3aded6MmREpF5kngei8Quq8BYq9bFy00jUlbDVErUiiczpzAm1_Qhi7GAPVhCMH65xH68IjEXv11dSD3l2ffgmeFrA</recordid><startdate>19730501</startdate><enddate>19730501</enddate><creator>Rowsell, E V</creator><creator>al-Tai, A H</creator><creator>Carnie, J A</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><scope>5PM</scope></search><sort><creationdate>19730501</creationdate><title>Increased liver L-serine-pyruvate aminotransferase activity under gluconeogenic conditions</title><author>Rowsell, E V ; al-Tai, A H ; Carnie, J A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c436t-77c4871f626482727474ed29eb17c02eb5d56667203b43d09ff6db2bf218f8c83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Aging</topic><topic>Alloxan - pharmacology</topic><topic>Animals</topic><topic>Animals, Newborn</topic><topic>Development</topic><topic>Female</topic><topic>Fetus</topic><topic>Glucagon - pharmacology</topic><topic>Gluconeogenesis</topic><topic>L-Serine Dehydratase - metabolism</topic><topic>Liver - drug effects</topic><topic>Liver - enzymology</topic><topic>Liver - growth & development</topic><topic>Pregnancy</topic><topic>Pyruvates</topic><topic>Rats</topic><topic>Serine</topic><topic>Transaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rowsell, E V</creatorcontrib><creatorcontrib>al-Tai, A H</creatorcontrib><creatorcontrib>Carnie, J A</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rowsell, E V</au><au>al-Tai, A H</au><au>Carnie, J A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Increased liver L-serine-pyruvate aminotransferase activity under gluconeogenic conditions</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1973-05-01</date><risdate>1973</risdate><volume>134</volume><issue>1</issue><spage>349</spage><epage>351</epage><pages>349-351</pages><issn>0264-6021</issn><issn>0306-3283</issn><eissn>1470-8728</eissn><abstract>Rat liver l-serine-pyruvate aminotransferase activity exceeds markedly the normal adult value (a) in the neonatal period, (b) after glucagon injection and (c) after alloxan injection, observations that reinforce the suggestion from comparative findings that the aminotransferase has a role in gluconeogenesis. Some findings, however, argue in favour of l-serine dehydratase as the enzyme of gluconeogenesis from l-serine.</abstract><cop>England</cop><pmid>4723229</pmid><doi>10.1042/bj1340349</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1973-05, Vol.134 (1), p.349-351 |
| issn | 0264-6021 0306-3283 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Aging Alloxan - pharmacology Animals Animals, Newborn Development Female Fetus Glucagon - pharmacology Gluconeogenesis L-Serine Dehydratase - metabolism Liver - drug effects Liver - enzymology Liver - growth & development Pregnancy Pyruvates Rats Serine Transaminases - metabolism |
| title | Increased liver L-serine-pyruvate aminotransferase activity under gluconeogenic conditions |
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