Purification and Catalytic Properties of Liver Alcohol Dehydrogenase Isoenzymes in Patients with Hepatoma in Nigeria
Alcohol dehydrogenase isoenzymes were isolated from the liver of patients with hepatoma and healthy control individuals. Whereas only a single form of the enzyme was obtained in healthy control liver, two distinct forms of the enzyme were found in hepatoma liver. These two forms were named AD-I and...
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| Veröffentlicht in: | Annals of clinical biochemistry 1993-03, Vol.30 (2), p.146-151 |
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| creator | Ogunleye, I O Olusi, S O |
| description | Alcohol dehydrogenase isoenzymes were isolated from the liver of patients with hepatoma and healthy control individuals. Whereas only a single form of the enzyme was obtained in healthy control liver, two distinct forms of the enzyme were found in hepatoma liver. These two forms were named AD-I and AD-II according to their elution pattern in CM-cellulose chromatography and mobility towards the anode in polyacrylamide gel electrophoresis. Both isoenzymes resembled normal liver enzyme with respect to their molecular properties. However, the two forms had distinct kinetic properties, although AD-I had some properties similar to the normal liver enzyme. The Km values of AD-I for ethanol, n-butanol and m-nitrobenzyl alcohol were 61μM, 90μM and 292μM, respectively, as against the values for AD-II which were 473μM, 100μM and 60μM for the respective substrates. Pyrazole inhibited the activity of AD-II but not that of AD-I. These kinetic properties of alcohol dehydrogenase in patients with hepatoma could be of clinical importance particularly in the tropics where the disease is prevalent. |
| doi_str_mv | 10.1177/000456329303000206 |
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Whereas only a single form of the enzyme was obtained in healthy control liver, two distinct forms of the enzyme were found in hepatoma liver. These two forms were named AD-I and AD-II according to their elution pattern in CM-cellulose chromatography and mobility towards the anode in polyacrylamide gel electrophoresis. Both isoenzymes resembled normal liver enzyme with respect to their molecular properties. However, the two forms had distinct kinetic properties, although AD-I had some properties similar to the normal liver enzyme. The Km values of AD-I for ethanol, n-butanol and m-nitrobenzyl alcohol were 61μM, 90μM and 292μM, respectively, as against the values for AD-II which were 473μM, 100μM and 60μM for the respective substrates. Pyrazole inhibited the activity of AD-II but not that of AD-I. These kinetic properties of alcohol dehydrogenase in patients with hepatoma could be of clinical importance particularly in the tropics where the disease is prevalent.</description><identifier>ISSN: 0004-5632</identifier><identifier>EISSN: 1758-1001</identifier><identifier>DOI: 10.1177/000456329303000206</identifier><identifier>PMID: 8385433</identifier><identifier>CODEN: ACBOBU</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><subject>Alcohol Dehydrogenase - isolation & purification ; Alcohol Dehydrogenase - physiology ; Analytical, structural and metabolic biochemistry ; Autopsy ; Biological and medical sciences ; Carcinoma, Hepatocellular - enzymology ; Chemical Fractionation ; Chromatography, Ion Exchange ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Humans ; Isoenzymes - isolation & purification ; Isoenzymes - physiology ; Liver - enzymology ; Liver Neoplasms - enzymology ; Nigeria ; Oxidoreductases ; Substrate Specificity</subject><ispartof>Annals of clinical biochemistry, 1993-03, Vol.30 (2), p.146-151</ispartof><rights>1993 Association for Clinical Biochemistry</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c367t-d3d21f8ded677dc270bda8421401ce39ce3f382624540550f226e234da0e934e3</citedby><cites>FETCH-LOGICAL-c367t-d3d21f8ded677dc270bda8421401ce39ce3f382624540550f226e234da0e934e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4654508$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8385433$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogunleye, I O</creatorcontrib><creatorcontrib>Olusi, S O</creatorcontrib><title>Purification and Catalytic Properties of Liver Alcohol Dehydrogenase Isoenzymes in Patients with Hepatoma in Nigeria</title><title>Annals of clinical biochemistry</title><addtitle>Ann Clin Biochem</addtitle><description>Alcohol dehydrogenase isoenzymes were isolated from the liver of patients with hepatoma and healthy control individuals. Whereas only a single form of the enzyme was obtained in healthy control liver, two distinct forms of the enzyme were found in hepatoma liver. These two forms were named AD-I and AD-II according to their elution pattern in CM-cellulose chromatography and mobility towards the anode in polyacrylamide gel electrophoresis. Both isoenzymes resembled normal liver enzyme with respect to their molecular properties. However, the two forms had distinct kinetic properties, although AD-I had some properties similar to the normal liver enzyme. The Km values of AD-I for ethanol, n-butanol and m-nitrobenzyl alcohol were 61μM, 90μM and 292μM, respectively, as against the values for AD-II which were 473μM, 100μM and 60μM for the respective substrates. Pyrazole inhibited the activity of AD-II but not that of AD-I. These kinetic properties of alcohol dehydrogenase in patients with hepatoma could be of clinical importance particularly in the tropics where the disease is prevalent.</description><subject>Alcohol Dehydrogenase - isolation & purification</subject><subject>Alcohol Dehydrogenase - physiology</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Autopsy</subject><subject>Biological and medical sciences</subject><subject>Carcinoma, Hepatocellular - enzymology</subject><subject>Chemical Fractionation</subject><subject>Chromatography, Ion Exchange</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - physiology</subject><subject>Liver - enzymology</subject><subject>Liver Neoplasms - enzymology</subject><subject>Nigeria</subject><subject>Oxidoreductases</subject><subject>Substrate Specificity</subject><issn>0004-5632</issn><issn>1758-1001</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9PGzEQxa0KBCn0C1Sq5APqbYv_7-aIQilIEeQA55WxZxOjXTvYXlD49PUqEZdKPYxmpPebN6OH0HdKflFa15eEECEVZ3NOeJkZUV_QjNayqSgh9AjNJqCaiFP0NaWXiakJOUEnDW-k4HyG8mqMrnNGZxc81t7ihc6632Vn8CqGLcTsIOHQ4aV7g4ivehM2ocfXsNnZGNbgdQJ8lwL4j91QSOfxqpiBzwm_u7zBt7DVOQx6Uu7dGqLT5-i4032Cb4d-hp5ufj8ubqvlw5-7xdWyMlzVubLcMto1Fqyqa2vK689WN4JRQagBPi_V8YYpJqQgUpKOMQWMC6sJzLkAfoZ-7n23MbyOkHI7uGSg77WHMKa2lkoJKXkB2R40MaQUoWu30Q067lpK2inq9t-oy9KPg_v4PID9XDlkW_SLg66T0X0XtTcufWJCSSFJU7DLPZb0GtqXMEZfMvnf4b8gGpOf</recordid><startdate>19930301</startdate><enddate>19930301</enddate><creator>Ogunleye, I O</creator><creator>Olusi, S O</creator><general>SAGE Publications</general><general>Royal Society of Medicine Press</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>19930301</creationdate><title>Purification and Catalytic Properties of Liver Alcohol Dehydrogenase Isoenzymes in Patients with Hepatoma in Nigeria</title><author>Ogunleye, I O ; Olusi, S O</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c367t-d3d21f8ded677dc270bda8421401ce39ce3f382624540550f226e234da0e934e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Alcohol Dehydrogenase - isolation & purification</topic><topic>Alcohol Dehydrogenase - physiology</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Autopsy</topic><topic>Biological and medical sciences</topic><topic>Carcinoma, Hepatocellular - enzymology</topic><topic>Chemical Fractionation</topic><topic>Chromatography, Ion Exchange</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - physiology</topic><topic>Liver - enzymology</topic><topic>Liver Neoplasms - enzymology</topic><topic>Nigeria</topic><topic>Oxidoreductases</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogunleye, I O</creatorcontrib><creatorcontrib>Olusi, S O</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>Annals of clinical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogunleye, I O</au><au>Olusi, S O</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Catalytic Properties of Liver Alcohol Dehydrogenase Isoenzymes in Patients with Hepatoma in Nigeria</atitle><jtitle>Annals of clinical biochemistry</jtitle><addtitle>Ann Clin Biochem</addtitle><date>1993-03-01</date><risdate>1993</risdate><volume>30</volume><issue>2</issue><spage>146</spage><epage>151</epage><pages>146-151</pages><issn>0004-5632</issn><eissn>1758-1001</eissn><coden>ACBOBU</coden><abstract>Alcohol dehydrogenase isoenzymes were isolated from the liver of patients with hepatoma and healthy control individuals. Whereas only a single form of the enzyme was obtained in healthy control liver, two distinct forms of the enzyme were found in hepatoma liver. These two forms were named AD-I and AD-II according to their elution pattern in CM-cellulose chromatography and mobility towards the anode in polyacrylamide gel electrophoresis. Both isoenzymes resembled normal liver enzyme with respect to their molecular properties. However, the two forms had distinct kinetic properties, although AD-I had some properties similar to the normal liver enzyme. The Km values of AD-I for ethanol, n-butanol and m-nitrobenzyl alcohol were 61μM, 90μM and 292μM, respectively, as against the values for AD-II which were 473μM, 100μM and 60μM for the respective substrates. Pyrazole inhibited the activity of AD-II but not that of AD-I. These kinetic properties of alcohol dehydrogenase in patients with hepatoma could be of clinical importance particularly in the tropics where the disease is prevalent.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><pmid>8385433</pmid><doi>10.1177/000456329303000206</doi><tpages>6</tpages></addata></record> |
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| ispartof | Annals of clinical biochemistry, 1993-03, Vol.30 (2), p.146-151 |
| issn | 0004-5632 1758-1001 |
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| subjects | Alcohol Dehydrogenase - isolation & purification Alcohol Dehydrogenase - physiology Analytical, structural and metabolic biochemistry Autopsy Biological and medical sciences Carcinoma, Hepatocellular - enzymology Chemical Fractionation Chromatography, Ion Exchange Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Isoenzymes - isolation & purification Isoenzymes - physiology Liver - enzymology Liver Neoplasms - enzymology Nigeria Oxidoreductases Substrate Specificity |
| title | Purification and Catalytic Properties of Liver Alcohol Dehydrogenase Isoenzymes in Patients with Hepatoma in Nigeria |
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