Adenosine aminohydrolase activity in the regenerating rat liver
The specific activity of adenosine aminohydrolase in the regenerating rat liver is significantly increased 12 h after partial hepatectomy. There is a twofold increase in enzyme activity at 48 h, after which the activity begins to decline. However, increased values still persist 7 days postsurgery. T...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1985-04, Vol.238 (1), p.259-262 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Sheid, Bertrum |
| description | The specific activity of adenosine aminohydrolase in the regenerating rat liver is significantly increased 12 h after partial hepatectomy. There is a twofold increase in enzyme activity at 48 h, after which the activity begins to decline. However, increased values still persist 7 days postsurgery. The enzyme is located mainly in the soluble supernatant (90–95%) of the cell. The purified enzyme from 48-h regenerating liver and control liver has similar kinetic properties (
K
m
54–58 μ
m for adenosine), similar molecular weights (30,000–35,000), and are equally inhibited by an irreversible transition-state analog and a reversible competitive inhibitor. It is concluded that adenosine aminohydrolase in regenerating liver is an integral component of a salvage pathway designed for the reutilization of nucleotides, and thus helps maintain a “growth state” for the regenerating liver. |
| doi_str_mv | 10.1016/0003-9861(85)90163-8 |
| format | Article |
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K
m
54–58 μ
m for adenosine), similar molecular weights (30,000–35,000), and are equally inhibited by an irreversible transition-state analog and a reversible competitive inhibitor. It is concluded that adenosine aminohydrolase in regenerating liver is an integral component of a salvage pathway designed for the reutilization of nucleotides, and thus helps maintain a “growth state” for the regenerating liver.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(85)90163-8</identifier><identifier>PMID: 3985621</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Adenosine Deaminase - metabolism ; Animals ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Liver - enzymology ; Liver Regeneration ; Liver. Bile. Biliary tracts ; Male ; Nucleoside Deaminases - metabolism ; Rats ; Rats, Inbred Strains ; Substrate Specificity ; Vertebrates: digestive system</subject><ispartof>Archives of biochemistry and biophysics, 1985-04, Vol.238 (1), p.259-262</ispartof><rights>1985</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-b0ace3ba0e8c0082114443756f630abbc51ed36dca53d8ca6f71c0622e994ae23</citedby><cites>FETCH-LOGICAL-c386t-b0ace3ba0e8c0082114443756f630abbc51ed36dca53d8ca6f71c0622e994ae23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986185901638$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8396165$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3985621$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sheid, Bertrum</creatorcontrib><title>Adenosine aminohydrolase activity in the regenerating rat liver</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The specific activity of adenosine aminohydrolase in the regenerating rat liver is significantly increased 12 h after partial hepatectomy. There is a twofold increase in enzyme activity at 48 h, after which the activity begins to decline. However, increased values still persist 7 days postsurgery. The enzyme is located mainly in the soluble supernatant (90–95%) of the cell. The purified enzyme from 48-h regenerating liver and control liver has similar kinetic properties (
K
m
54–58 μ
m for adenosine), similar molecular weights (30,000–35,000), and are equally inhibited by an irreversible transition-state analog and a reversible competitive inhibitor. It is concluded that adenosine aminohydrolase in regenerating liver is an integral component of a salvage pathway designed for the reutilization of nucleotides, and thus helps maintain a “growth state” for the regenerating liver.</description><subject>Adenosine Deaminase - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>Liver Regeneration</subject><subject>Liver. Bile. Biliary tracts</subject><subject>Male</subject><subject>Nucleoside Deaminases - metabolism</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Substrate Specificity</subject><subject>Vertebrates: digestive system</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AQhhdRaq3-A4UcRPQQnc1mt5uLUopfUPCi52WzmbQryabupoX-exMbevQ0zMwzw8tDyCWFewpUPAAAizMp6K3kd1k3YbE8ImMKmYiByfSYjA_IKTkL4RuA0lQkIzJimeQioWPyNCvQNcE6jHRtXbPaFb6pdOha09qtbXeRdVG7wsjjEh163Vq3jLoSVXaL_pyclLoKeDHUCfl6ef6cv8WLj9f3-WwRGyZFG-egDbJcA0oDIJMuR5qyKRelYKDz3HCKBROF0ZwV0mhRTqkBkSSYZanGhE3Izf7v2jc_Gwytqm0wWFXaYbMJaiqAc5H1YLoHjW9C8Fiqtbe19jtFQfXeVC9F9VKU5OrPm5Ld2dXwf5PXWByOBlHd_nrY62B0VXrtjA0HTLJMUME77HGPYedia9GrYCw6g4X1aFpVNPb_HL8fbIkY</recordid><startdate>198504</startdate><enddate>198504</enddate><creator>Sheid, Bertrum</creator><general>Elsevier Inc</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>198504</creationdate><title>Adenosine aminohydrolase activity in the regenerating rat liver</title><author>Sheid, Bertrum</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-b0ace3ba0e8c0082114443756f630abbc51ed36dca53d8ca6f71c0622e994ae23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Adenosine Deaminase - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Liver Regeneration</topic><topic>Liver. Bile. Biliary tracts</topic><topic>Male</topic><topic>Nucleoside Deaminases - metabolism</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Substrate Specificity</topic><topic>Vertebrates: digestive system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sheid, Bertrum</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sheid, Bertrum</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adenosine aminohydrolase activity in the regenerating rat liver</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1985-04</date><risdate>1985</risdate><volume>238</volume><issue>1</issue><spage>259</spage><epage>262</epage><pages>259-262</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>The specific activity of adenosine aminohydrolase in the regenerating rat liver is significantly increased 12 h after partial hepatectomy. There is a twofold increase in enzyme activity at 48 h, after which the activity begins to decline. However, increased values still persist 7 days postsurgery. The enzyme is located mainly in the soluble supernatant (90–95%) of the cell. The purified enzyme from 48-h regenerating liver and control liver has similar kinetic properties (
K
m
54–58 μ
m for adenosine), similar molecular weights (30,000–35,000), and are equally inhibited by an irreversible transition-state analog and a reversible competitive inhibitor. It is concluded that adenosine aminohydrolase in regenerating liver is an integral component of a salvage pathway designed for the reutilization of nucleotides, and thus helps maintain a “growth state” for the regenerating liver.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3985621</pmid><doi>10.1016/0003-9861(85)90163-8</doi><tpages>4</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1985-04, Vol.238 (1), p.259-262 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Deaminase - metabolism Animals Biological and medical sciences Fundamental and applied biological sciences. Psychology Kinetics Liver - enzymology Liver Regeneration Liver. Bile. Biliary tracts Male Nucleoside Deaminases - metabolism Rats Rats, Inbred Strains Substrate Specificity Vertebrates: digestive system |
| title | Adenosine aminohydrolase activity in the regenerating rat liver |
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