Reactivation of apo liver alcohol dehydrogenase with lead, mercury and cadmium
Liver alcohol dehydrogenase is a dimer of 80,000 M sub(r) with one structural and one catalytic zinc atom per subunit. It is possible to substitute either one or both zinc atoms by different methods. Within each liver alcohol dehydrogenase molecule, there are 2 subunits, 2 active sites and 4 zinc at...
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| Veröffentlicht in: | FEBS letters 1982-01, Vol.137 (2), p.257-260 |
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| creator | Skjeldal, L. Dahl, K.H. McKinley-McKee, J.S. |
| description | Liver alcohol dehydrogenase is a dimer of 80,000 M sub(r) with one structural and one catalytic zinc atom per subunit. It is possible to substitute either one or both zinc atoms by different methods. Within each liver alcohol dehydrogenase molecule, there are 2 subunits, 2 active sites and 4 zinc atoms, 2 catalytic (c) and 2 structural or non catalytic (n). The native enzyme is consequently written Zn(c) sub(2)Zn(n) sub(2). Removal of metal is designated by apo. Thus apo(c) sub(2)Zn(n) sub(2) represents enzyme with the catalytic zinc atoms removed. It is often most convenient to make the "hybrid-enzyme", Me(c) sub(2)Zn(n) sub(2), from the "apohybrid", apo(c) sub(2)Zn(n) sub(2), since this is more stable than the fully depleted enzyme, apo(c) sub(2)apo(n) sub(2). The authors show that activity can be restored to dissolved apo liver alcohol dehydrogenase, apo(c) sub(2)Zn(N) sub(2), with the heavy metals cadmium, mercury and lead. |
| doi_str_mv | 10.1016/0014-5793(82)80362-1 |
| format | Article |
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It is possible to substitute either one or both zinc atoms by different methods. Within each liver alcohol dehydrogenase molecule, there are 2 subunits, 2 active sites and 4 zinc atoms, 2 catalytic (c) and 2 structural or non catalytic (n). The native enzyme is consequently written Zn(c) sub(2)Zn(n) sub(2). Removal of metal is designated by apo. Thus apo(c) sub(2)Zn(n) sub(2) represents enzyme with the catalytic zinc atoms removed. It is often most convenient to make the "hybrid-enzyme", Me(c) sub(2)Zn(n) sub(2), from the "apohybrid", apo(c) sub(2)Zn(n) sub(2), since this is more stable than the fully depleted enzyme, apo(c) sub(2)apo(n) sub(2). The authors show that activity can be restored to dissolved apo liver alcohol dehydrogenase, apo(c) sub(2)Zn(N) sub(2), with the heavy metals cadmium, mercury and lead.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(82)80362-1</identifier><identifier>PMID: 7037457</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Alcohol Dehydrogenase ; Alcohol Oxidoreductases - metabolism ; Animals ; Apoenzymes - metabolism ; Apoproteins - metabolism ; cadmium ; Cadmium - pharmacology ; Enzyme Activation ; Enzyme Reactivators ; Horses ; Kinetics ; lead ; Lead - pharmacology ; liver ; Liver - enzymology ; mercury ; Mercury - pharmacology ; Spectrophotometry, Ultraviolet</subject><ispartof>FEBS letters, 1982-01, Vol.137 (2), p.257-260</ispartof><rights>1982</rights><rights>FEBS Letters 137 (1982) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4971-8075e215b42f594d22553ffd2814354c07dbb82d5c88f3c8c90ef1c9abcbcc53</citedby><cites>FETCH-LOGICAL-c4971-8075e215b42f594d22553ffd2814354c07dbb82d5c88f3c8c90ef1c9abcbcc53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579382803621$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7037457$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Skjeldal, L.</creatorcontrib><creatorcontrib>Dahl, K.H.</creatorcontrib><creatorcontrib>McKinley-McKee, J.S.</creatorcontrib><title>Reactivation of apo liver alcohol dehydrogenase with lead, mercury and cadmium</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Liver alcohol dehydrogenase is a dimer of 80,000 M sub(r) with one structural and one catalytic zinc atom per subunit. It is possible to substitute either one or both zinc atoms by different methods. Within each liver alcohol dehydrogenase molecule, there are 2 subunits, 2 active sites and 4 zinc atoms, 2 catalytic (c) and 2 structural or non catalytic (n). The native enzyme is consequently written Zn(c) sub(2)Zn(n) sub(2). Removal of metal is designated by apo. Thus apo(c) sub(2)Zn(n) sub(2) represents enzyme with the catalytic zinc atoms removed. It is often most convenient to make the "hybrid-enzyme", Me(c) sub(2)Zn(n) sub(2), from the "apohybrid", apo(c) sub(2)Zn(n) sub(2), since this is more stable than the fully depleted enzyme, apo(c) sub(2)apo(n) sub(2). The authors show that activity can be restored to dissolved apo liver alcohol dehydrogenase, apo(c) sub(2)Zn(N) sub(2), with the heavy metals cadmium, mercury and lead.</description><subject>Alcohol Dehydrogenase</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Animals</subject><subject>Apoenzymes - metabolism</subject><subject>Apoproteins - metabolism</subject><subject>cadmium</subject><subject>Cadmium - pharmacology</subject><subject>Enzyme Activation</subject><subject>Enzyme Reactivators</subject><subject>Horses</subject><subject>Kinetics</subject><subject>lead</subject><subject>Lead - pharmacology</subject><subject>liver</subject><subject>Liver - enzymology</subject><subject>mercury</subject><subject>Mercury - pharmacology</subject><subject>Spectrophotometry, Ultraviolet</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE9v1DAQxS0EKtvCNwDJJ0QlAv67di6VoOoCUgUS6t1yxhPWKIkXO9lqvz1Jd9UjcBrNvDdvRj9CXnH2njO-_sAYV5U2tXxrxaVlci0q_oSsuDWykmptn5LVo-U5OS_lF5t7y-szcmaYNEqbFfn2Az2Mce_HmAaaWup3iXZxj5n6DtI2dTTg9hBy-omDL0jv47ilHfrwjvaYYcoH6odAwYc-Tv0L8qz1XcGXp3pB7jY3d9dfqtvvn79ef7ytQNWGV5YZjYLrRolW1yoIobVs2yAsV1IrYCY0jRVBg7WtBAs1w5ZD7RtoALS8IG-Osbucfk9YRtfHAth1fsA0FWdkbfSay38auVYzLslnozoaIadSMrZul2Pv88Fx5hbcbmHpFpbOCveA2y1rr0_5U9NjeFw68Z31zVG_jx0e_ivTbW4-iUVY5lY8TJdDV8cgnKnuI2ZXIOIAGGJGGF1I8e-f_gGre6Gh</recordid><startdate>19820125</startdate><enddate>19820125</enddate><creator>Skjeldal, L.</creator><creator>Dahl, K.H.</creator><creator>McKinley-McKee, J.S.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19820125</creationdate><title>Reactivation of apo liver alcohol dehydrogenase with lead, mercury and cadmium</title><author>Skjeldal, L. ; Dahl, K.H. ; McKinley-McKee, J.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4971-8075e215b42f594d22553ffd2814354c07dbb82d5c88f3c8c90ef1c9abcbcc53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Alcohol Dehydrogenase</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Animals</topic><topic>Apoenzymes - metabolism</topic><topic>Apoproteins - metabolism</topic><topic>cadmium</topic><topic>Cadmium - pharmacology</topic><topic>Enzyme Activation</topic><topic>Enzyme Reactivators</topic><topic>Horses</topic><topic>Kinetics</topic><topic>lead</topic><topic>Lead - pharmacology</topic><topic>liver</topic><topic>Liver - enzymology</topic><topic>mercury</topic><topic>Mercury - pharmacology</topic><topic>Spectrophotometry, Ultraviolet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Skjeldal, L.</creatorcontrib><creatorcontrib>Dahl, K.H.</creatorcontrib><creatorcontrib>McKinley-McKee, J.S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Skjeldal, L.</au><au>Dahl, K.H.</au><au>McKinley-McKee, J.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reactivation of apo liver alcohol dehydrogenase with lead, mercury and cadmium</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1982-01-25</date><risdate>1982</risdate><volume>137</volume><issue>2</issue><spage>257</spage><epage>260</epage><pages>257-260</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Liver alcohol dehydrogenase is a dimer of 80,000 M sub(r) with one structural and one catalytic zinc atom per subunit. It is possible to substitute either one or both zinc atoms by different methods. Within each liver alcohol dehydrogenase molecule, there are 2 subunits, 2 active sites and 4 zinc atoms, 2 catalytic (c) and 2 structural or non catalytic (n). The native enzyme is consequently written Zn(c) sub(2)Zn(n) sub(2). Removal of metal is designated by apo. Thus apo(c) sub(2)Zn(n) sub(2) represents enzyme with the catalytic zinc atoms removed. It is often most convenient to make the "hybrid-enzyme", Me(c) sub(2)Zn(n) sub(2), from the "apohybrid", apo(c) sub(2)Zn(n) sub(2), since this is more stable than the fully depleted enzyme, apo(c) sub(2)apo(n) sub(2). The authors show that activity can be restored to dissolved apo liver alcohol dehydrogenase, apo(c) sub(2)Zn(N) sub(2), with the heavy metals cadmium, mercury and lead.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7037457</pmid><doi>10.1016/0014-5793(82)80362-1</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1982-01, Vol.137 (2), p.257-260 |
| issn | 0014-5793 1873-3468 |
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| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Alcohol Dehydrogenase Alcohol Oxidoreductases - metabolism Animals Apoenzymes - metabolism Apoproteins - metabolism cadmium Cadmium - pharmacology Enzyme Activation Enzyme Reactivators Horses Kinetics lead Lead - pharmacology liver Liver - enzymology mercury Mercury - pharmacology Spectrophotometry, Ultraviolet |
| title | Reactivation of apo liver alcohol dehydrogenase with lead, mercury and cadmium |
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