Chemical cross-linking of mitochondrial NADH dehydrogenase from bovine heart
The structure of bovine heart mitochondrial NADH dehydrogenase was investigated by using two cleavable cross-linking agents, disuccinimidyl tartrate and (ethylene glycol)yl bis-(succinimidyl succinate). Cross-linking was analysed primarily by immunoblotting to detect products containing subunits of...
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| Veröffentlicht in: | Biochemical journal 1985-01, Vol.227 (2), p.467-474 |
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| container_end_page | 474 |
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| container_title | Biochemical journal |
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| creator | Cleeter, M.W.J Banister, S.H Ragan, C.I |
| description | The structure of bovine heart mitochondrial NADH dehydrogenase was investigated by using two cleavable cross-linking agents, disuccinimidyl tartrate and (ethylene glycol)yl bis-(succinimidyl succinate). Cross-linking was analysed primarily by immunoblotting to detect products containing subunits of the iron-protein fraction from chaotropic resolution of the enzyme, namely those of 75, 49, 30 and 13 kDa. By using both the isolated iron-protein fraction and the intact dehydrogenase, cross-links were identified between these four subunits, from these subunits to the largest subunit of the flavoprotein fraction, which contains the active site for NADH, and from these subunits to polypeptides in the hydrophobic shell, which surrounds the hydrophilic iron-protein and flavoprotein fractions. |
| doi_str_mv | 10.1042/bj2270467 |
| format | Article |
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Cross-linking was analysed primarily by immunoblotting to detect products containing subunits of the iron-protein fraction from chaotropic resolution of the enzyme, namely those of 75, 49, 30 and 13 kDa. By using both the isolated iron-protein fraction and the intact dehydrogenase, cross-links were identified between these four subunits, from these subunits to the largest subunit of the flavoprotein fraction, which contains the active site for NADH, and from these subunits to polypeptides in the hydrophobic shell, which surrounds the hydrophilic iron-protein and flavoprotein fractions.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2270467</identifier><identifier>PMID: 4004775</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Binding Sites ; Cattle ; cross-linking ; Cross-Linking Reagents ; Cytochrome Reductases - immunology ; disuccinimidyl tartrate ; Electrophoresis, Polyacrylamide Gel ; ethylene glycolyl bis-(succinimidyl succinate) ; heart ; Metalloproteins - analysis ; mitochondria ; Mitochondria, Heart - enzymology ; NAD ; NAD (coenzyme) ; NADH dehydrogenase ; NADH Dehydrogenase - immunology ; oxidoreductases ; subunit structure ; Succinimides</subject><ispartof>Biochemical journal, 1985-01, Vol.227 (2), p.467-474</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-6c6a3b3cf86b64f2264b820c4dc491e020d9788398f3a1dc05d57124e03a5d603</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/PMC1144865/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1144865/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4004775$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cleeter, M.W.J</creatorcontrib><creatorcontrib>Banister, S.H</creatorcontrib><creatorcontrib>Ragan, C.I</creatorcontrib><title>Chemical cross-linking of mitochondrial NADH dehydrogenase from bovine heart</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>The structure of bovine heart mitochondrial NADH dehydrogenase was investigated by using two cleavable cross-linking agents, disuccinimidyl tartrate and (ethylene glycol)yl bis-(succinimidyl succinate). Cross-linking was analysed primarily by immunoblotting to detect products containing subunits of the iron-protein fraction from chaotropic resolution of the enzyme, namely those of 75, 49, 30 and 13 kDa. By using both the isolated iron-protein fraction and the intact dehydrogenase, cross-links were identified between these four subunits, from these subunits to the largest subunit of the flavoprotein fraction, which contains the active site for NADH, and from these subunits to polypeptides in the hydrophobic shell, which surrounds the hydrophilic iron-protein and flavoprotein fractions.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Cattle</subject><subject>cross-linking</subject><subject>Cross-Linking Reagents</subject><subject>Cytochrome Reductases - immunology</subject><subject>disuccinimidyl tartrate</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>ethylene glycolyl bis-(succinimidyl succinate)</subject><subject>heart</subject><subject>Metalloproteins - analysis</subject><subject>mitochondria</subject><subject>Mitochondria, Heart - enzymology</subject><subject>NAD</subject><subject>NAD (coenzyme)</subject><subject>NADH dehydrogenase</subject><subject>NADH Dehydrogenase - immunology</subject><subject>oxidoreductases</subject><subject>subunit structure</subject><subject>Succinimides</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi1EVZbCgR-AyAmJQ-jYHn_kglQtH0ValQP0bDm2s3FJ4mJnK_Xfk7KrFZzoaQ7vo1cz8xDyisJ7CsjO2xvGFKBUT8iKooJaK6afkhUwibUERp-R56XcAFAEhFNyigColFiRzboPY3R2qFxOpdRDnH7GaVulrhrjnFyfJp_jEl9dfLysfOjvfU7bMNkSqi6nsWrTXZxC1Qeb5xfkpLNDCS8P84xcf_70Y31Zb759-bq-2NQOhZxr6aTlLXedlq3Eji1LtpqBQ--woQEY-EZpzRvdcUu9A-GFogwDcCu8BH5GPux7b3ftGLwL05ztYG5zHG2-N8lG828yxd5s052hFFFLsRS8PRTk9GsXymzGWFwYBjuFtCtGSSpoo_C_IEXeKFDqESAVAkEu4Ls9-OffOXTHtSmYB5nmKHNhX_9955E82FvyN_u8s8nYbY7FXH9nQPmDd8WU5r8BO7GiuA</recordid><startdate>19850101</startdate><enddate>19850101</enddate><creator>Cleeter, M.W.J</creator><creator>Banister, S.H</creator><creator>Ragan, C.I</creator><scope>FBQ</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><scope>5PM</scope></search><sort><creationdate>19850101</creationdate><title>Chemical cross-linking of mitochondrial NADH dehydrogenase from bovine heart</title><author>Cleeter, M.W.J ; Banister, S.H ; Ragan, C.I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-6c6a3b3cf86b64f2264b820c4dc491e020d9788398f3a1dc05d57124e03a5d603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Cattle</topic><topic>cross-linking</topic><topic>Cross-Linking Reagents</topic><topic>Cytochrome Reductases - immunology</topic><topic>disuccinimidyl tartrate</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>ethylene glycolyl bis-(succinimidyl succinate)</topic><topic>heart</topic><topic>Metalloproteins - analysis</topic><topic>mitochondria</topic><topic>Mitochondria, Heart - enzymology</topic><topic>NAD</topic><topic>NAD (coenzyme)</topic><topic>NADH dehydrogenase</topic><topic>NADH Dehydrogenase - immunology</topic><topic>oxidoreductases</topic><topic>subunit structure</topic><topic>Succinimides</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cleeter, M.W.J</creatorcontrib><creatorcontrib>Banister, S.H</creatorcontrib><creatorcontrib>Ragan, C.I</creatorcontrib><collection>AGRIS</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cleeter, M.W.J</au><au>Banister, S.H</au><au>Ragan, C.I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chemical cross-linking of mitochondrial NADH dehydrogenase from bovine heart</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1985-01-01</date><risdate>1985</risdate><volume>227</volume><issue>2</issue><spage>467</spage><epage>474</epage><pages>467-474</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The structure of bovine heart mitochondrial NADH dehydrogenase was investigated by using two cleavable cross-linking agents, disuccinimidyl tartrate and (ethylene glycol)yl bis-(succinimidyl succinate). Cross-linking was analysed primarily by immunoblotting to detect products containing subunits of the iron-protein fraction from chaotropic resolution of the enzyme, namely those of 75, 49, 30 and 13 kDa. By using both the isolated iron-protein fraction and the intact dehydrogenase, cross-links were identified between these four subunits, from these subunits to the largest subunit of the flavoprotein fraction, which contains the active site for NADH, and from these subunits to polypeptides in the hydrophobic shell, which surrounds the hydrophilic iron-protein and flavoprotein fractions.</abstract><cop>England</cop><pmid>4004775</pmid><doi>10.1042/bj2270467</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1985-01, Vol.227 (2), p.467-474 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Binding Sites Cattle cross-linking Cross-Linking Reagents Cytochrome Reductases - immunology disuccinimidyl tartrate Electrophoresis, Polyacrylamide Gel ethylene glycolyl bis-(succinimidyl succinate) heart Metalloproteins - analysis mitochondria Mitochondria, Heart - enzymology NAD NAD (coenzyme) NADH dehydrogenase NADH Dehydrogenase - immunology oxidoreductases subunit structure Succinimides |
| title | Chemical cross-linking of mitochondrial NADH dehydrogenase from bovine heart |
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