Calcium binding to polypeptides of rat liver and Zajdela hepatoma mitochondrial inner membranes
Composition and amount of 45Ca 2+-binding proteins in the inner membrane fraction of rat liver and Zajdela hepatoma mitochondria were determined. In the inner membrane of liver mitochondria, three major 45Ca 2+-binding polypeptides: a protein of ∼130 kDa (carbamoyl-phosphate synthetase), a glycoprot...
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| Veröffentlicht in: | FEBS letters 1998-02, Vol.423 (1), p.45-48 |
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| creator | Evtodienko, Yuri V Azarashvili, Tamara S Kudin, Alexei P |
| description | Composition and amount of
45Ca
2+-binding proteins in the inner membrane fraction of rat liver and Zajdela hepatoma mitochondria were determined. In the inner membrane of liver mitochondria, three major
45Ca
2+-binding polypeptides: a protein of ∼130 kDa (carbamoyl-phosphate synthetase), a glycoprotein of 43–44 kDa (previously considered as the calcium uniporter), and 29–30 kDa protein were found. These components were absent (130 kDa component) or relatively reduced (43–44 kDa and 29–30 kDa components) in the inner membrane of hepatoma mitochondria. Previously unknown low molecular mass polypeptides, having very high Ca
2+-binding ability, were found in the inner membrane of hepatoma mitochondria. One of them might be the natural Ca
2+-binding inhibitor of H
+-ATPase. |
| doi_str_mv | 10.1016/S0014-5793(98)00059-3 |
| format | Article |
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45Ca
2+-binding proteins in the inner membrane fraction of rat liver and Zajdela hepatoma mitochondria were determined. In the inner membrane of liver mitochondria, three major
45Ca
2+-binding polypeptides: a protein of ∼130 kDa (carbamoyl-phosphate synthetase), a glycoprotein of 43–44 kDa (previously considered as the calcium uniporter), and 29–30 kDa protein were found. These components were absent (130 kDa component) or relatively reduced (43–44 kDa and 29–30 kDa components) in the inner membrane of hepatoma mitochondria. Previously unknown low molecular mass polypeptides, having very high Ca
2+-binding ability, were found in the inner membrane of hepatoma mitochondria. One of them might be the natural Ca
2+-binding inhibitor of H
+-ATPase.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)00059-3</identifier><identifier>PMID: 9506839</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Ca 2+-binding protein ; Ca2+-binding protein ; CaBI, Ca2+-binding inhibitor protein of H+-ATPase ; Calcium-Binding Proteins - analysis ; Carcinoma, Hepatocellular ; Cells, Cultured ; Hepatoma cell ; IMM, inner mitochondrial membrane ; Intracellular Membranes - chemistry ; Liver - chemistry ; Liver - cytology ; Liver cell ; LMM CaBP, low molecular mass Ca2+-binding protein ; Male ; Membrane Proteins - analysis ; Mitochondria - chemistry ; Mitochondrion ; Peptides - analysis ; PTP, permeability transition pore ; Rats ; Rats, Wistar ; Tumor Cells, Cultured</subject><ispartof>FEBS letters, 1998-02, Vol.423 (1), p.45-48</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 423 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4723-207fc2815bdb2005efd09f864c81edd76ac96c396c17190ff557de8c7dbebfce3</citedby><cites>FETCH-LOGICAL-c4723-207fc2815bdb2005efd09f864c81edd76ac96c396c17190ff557de8c7dbebfce3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2898%2900059-3$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579398000593$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9506839$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Evtodienko, Yuri V</creatorcontrib><creatorcontrib>Azarashvili, Tamara S</creatorcontrib><creatorcontrib>Kudin, Alexei P</creatorcontrib><title>Calcium binding to polypeptides of rat liver and Zajdela hepatoma mitochondrial inner membranes</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Composition and amount of
45Ca
2+-binding proteins in the inner membrane fraction of rat liver and Zajdela hepatoma mitochondria were determined. In the inner membrane of liver mitochondria, three major
45Ca
2+-binding polypeptides: a protein of ∼130 kDa (carbamoyl-phosphate synthetase), a glycoprotein of 43–44 kDa (previously considered as the calcium uniporter), and 29–30 kDa protein were found. These components were absent (130 kDa component) or relatively reduced (43–44 kDa and 29–30 kDa components) in the inner membrane of hepatoma mitochondria. Previously unknown low molecular mass polypeptides, having very high Ca
2+-binding ability, were found in the inner membrane of hepatoma mitochondria. One of them might be the natural Ca
2+-binding inhibitor of H
+-ATPase.</description><subject>Animals</subject><subject>Ca 2+-binding protein</subject><subject>Ca2+-binding protein</subject><subject>CaBI, Ca2+-binding inhibitor protein of H+-ATPase</subject><subject>Calcium-Binding Proteins - analysis</subject><subject>Carcinoma, Hepatocellular</subject><subject>Cells, Cultured</subject><subject>Hepatoma cell</subject><subject>IMM, inner mitochondrial membrane</subject><subject>Intracellular Membranes - chemistry</subject><subject>Liver - chemistry</subject><subject>Liver - cytology</subject><subject>Liver cell</subject><subject>LMM CaBP, low molecular mass Ca2+-binding protein</subject><subject>Male</subject><subject>Membrane Proteins - analysis</subject><subject>Mitochondria - chemistry</subject><subject>Mitochondrion</subject><subject>Peptides - analysis</subject><subject>PTP, permeability transition pore</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Tumor Cells, Cultured</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFP3DAQhS1EBVvgJyD5hOghYMdJbJ8QXUFBQuqh5cLFcuwxGDlxsLNU---b7K64wmFkad6bN-MPoVNKLiihzeUfQmhV1Fyycyl-EEJqWbA9tKCCs4JVjdhHiw_LIfqe8-tkooLKA3Qga9IIJhdILXUwftXh1vfW9894jHiIYT3AMHoLGUeHkx5x8O-QsO4tftKvFoLGLzDoMXYad36M5iX2NnkdsO_7ydhB1ybdQz5G35wOGU527xF6vL35u7wrHn7_ul9ePxSm4iUrSsKdKQWtW9uW01fAWSKdaCojKFjLG21kY9hUlFNJnKtrbkEYbltonQF2hM62uUOKbyvIo-p8NhDCdERcZcUlZ6RibDLWW6NJMecETg3JdzqtFSVqBqs2YNVMTUmhNmDVPHe6W7BqO7AfUzuSk3631f_5AOuvharbm5_lRpkFKTbtedXVNgomYO8eksrGQ2_A-gRmVDb6T479D_bYncI</recordid><startdate>19980213</startdate><enddate>19980213</enddate><creator>Evtodienko, Yuri V</creator><creator>Azarashvili, Tamara S</creator><creator>Kudin, Alexei P</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>7X8</scope></search><sort><creationdate>19980213</creationdate><title>Calcium binding to polypeptides of rat liver and Zajdela hepatoma mitochondrial inner membranes</title><author>Evtodienko, Yuri V ; Azarashvili, Tamara S ; Kudin, Alexei P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4723-207fc2815bdb2005efd09f864c81edd76ac96c396c17190ff557de8c7dbebfce3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Ca 2+-binding protein</topic><topic>Ca2+-binding protein</topic><topic>CaBI, Ca2+-binding inhibitor protein of H+-ATPase</topic><topic>Calcium-Binding Proteins - analysis</topic><topic>Carcinoma, Hepatocellular</topic><topic>Cells, Cultured</topic><topic>Hepatoma cell</topic><topic>IMM, inner mitochondrial membrane</topic><topic>Intracellular Membranes - chemistry</topic><topic>Liver - chemistry</topic><topic>Liver - cytology</topic><topic>Liver cell</topic><topic>LMM CaBP, low molecular mass Ca2+-binding protein</topic><topic>Male</topic><topic>Membrane Proteins - analysis</topic><topic>Mitochondria - chemistry</topic><topic>Mitochondrion</topic><topic>Peptides - analysis</topic><topic>PTP, permeability transition pore</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Evtodienko, Yuri V</creatorcontrib><creatorcontrib>Azarashvili, Tamara S</creatorcontrib><creatorcontrib>Kudin, Alexei P</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Evtodienko, Yuri V</au><au>Azarashvili, Tamara S</au><au>Kudin, Alexei P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calcium binding to polypeptides of rat liver and Zajdela hepatoma mitochondrial inner membranes</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-02-13</date><risdate>1998</risdate><volume>423</volume><issue>1</issue><spage>45</spage><epage>48</epage><pages>45-48</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Composition and amount of
45Ca
2+-binding proteins in the inner membrane fraction of rat liver and Zajdela hepatoma mitochondria were determined. In the inner membrane of liver mitochondria, three major
45Ca
2+-binding polypeptides: a protein of ∼130 kDa (carbamoyl-phosphate synthetase), a glycoprotein of 43–44 kDa (previously considered as the calcium uniporter), and 29–30 kDa protein were found. These components were absent (130 kDa component) or relatively reduced (43–44 kDa and 29–30 kDa components) in the inner membrane of hepatoma mitochondria. Previously unknown low molecular mass polypeptides, having very high Ca
2+-binding ability, were found in the inner membrane of hepatoma mitochondria. One of them might be the natural Ca
2+-binding inhibitor of H
+-ATPase.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9506839</pmid><doi>10.1016/S0014-5793(98)00059-3</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0014-5793 1873-3468 |
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| source | Wiley Free Content; MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Ca 2+-binding protein Ca2+-binding protein CaBI, Ca2+-binding inhibitor protein of H+-ATPase Calcium-Binding Proteins - analysis Carcinoma, Hepatocellular Cells, Cultured Hepatoma cell IMM, inner mitochondrial membrane Intracellular Membranes - chemistry Liver - chemistry Liver - cytology Liver cell LMM CaBP, low molecular mass Ca2+-binding protein Male Membrane Proteins - analysis Mitochondria - chemistry Mitochondrion Peptides - analysis PTP, permeability transition pore Rats Rats, Wistar Tumor Cells, Cultured |
| title | Calcium binding to polypeptides of rat liver and Zajdela hepatoma mitochondrial inner membranes |
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