Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin
Cleavage of natural inhibitor of mitochondrial ATPase by thrombin occurs at two specific sites. First an Arg-Ser bond is split giving two peptides. The main peptide which retains integral biological activity is further cleaved at two successive Arg-Ala bonds, none of the products is able to inhibit...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1982-07, Vol.107 (2), p.435-441 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Dianoux, A.-C. Freyssinet, J.-M. |
| description | Cleavage of natural inhibitor of mitochondrial ATPase by thrombin occurs at two specific sites. First an Arg-Ser bond is split giving two peptides. The main peptide which retains integral biological activity is further cleaved at two successive Arg-Ala bonds, none of the products is able to inhibit ATPase. The isolation of these peptides and their characterization are described. |
| doi_str_mv | 10.1016/0006-291X(82)91510-8 |
| format | Article |
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The isolation of these peptides and their characterization are described.</description><subject>Adenosine Triphosphatases - antagonists & inhibitors</subject><subject>adenosinetriphosphatase inhibitor</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>ATPase Inhibitory Protein</subject><subject>Cattle</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Horses</subject><subject>Humans</subject><subject>Mitochondria, Heart - analysis</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - analysis</subject><subject>Proteins - metabolism</subject><subject>thrombin</subject><subject>Thrombin - pharmacology</subject><subject>Time Factors</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE9rGzEQxUVocBw336CBPZXmsMmM9o-0l0IwSVsIJJAUchNaaVQreFeOtC7k22c3Nj62pxnmvXkz_Bj7gnCJgPUVANQ5b_D5m-QXDVYIuTxic4QGco5QfmLzg-WEnab0AoBY1s2MzWqOFRRizu4fN2S88yZzUf_pqB_04EOfBZf1ethGvc58v_KtH0Kcht3YmFXobfSjdP30oBNl7Vs2rGLoWt9_ZsdOrxOd7euC_b69eVr-zO_uf_xaXt_lppByyElUVluNjaXxIYktJ4NoOfGKNIeiLoRwrQaHheC1LYQDo60TBmpoJJliwb7ucjcxvG4pDarzydB6rXsK26REyUuOQv7XiFVVSV7jaCx3RhNDSpGc2kTf6fimENQEXE001URTSa4-gKsp_3yfv207soelPeFR_77TaaTx11NUyXjqDVkfyQzKBv_vA-9rA5Ar</recordid><startdate>19820730</startdate><enddate>19820730</enddate><creator>Dianoux, A.-C.</creator><creator>Freyssinet, J.-M.</creator><general>Elsevier Inc</general><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>19820730</creationdate><title>Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin</title><author>Dianoux, A.-C. ; Freyssinet, J.-M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-e75dada19de46981b2ec11d2e25ea2036377fba0f13726d37f0cadf7c06098ec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Adenosine Triphosphatases - antagonists & inhibitors</topic><topic>adenosinetriphosphatase inhibitor</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>ATPase Inhibitory Protein</topic><topic>Cattle</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Horses</topic><topic>Humans</topic><topic>Mitochondria, Heart - analysis</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - analysis</topic><topic>Proteins - metabolism</topic><topic>thrombin</topic><topic>Thrombin - pharmacology</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dianoux, A.-C.</creatorcontrib><creatorcontrib>Freyssinet, J.-M.</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dianoux, A.-C.</au><au>Freyssinet, J.-M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1982-07-30</date><risdate>1982</risdate><volume>107</volume><issue>2</issue><spage>435</spage><epage>441</epage><pages>435-441</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Cleavage of natural inhibitor of mitochondrial ATPase by thrombin occurs at two specific sites. 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| ispartof | Biochemical and biophysical research communications, 1982-07, Vol.107 (2), p.435-441 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Adenosine Triphosphatases - antagonists & inhibitors adenosinetriphosphatase inhibitor Amino Acid Sequence Animals ATPase Inhibitory Protein Cattle Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Horses Humans Mitochondria, Heart - analysis Molecular Weight Peptide Fragments - analysis Proteins - metabolism thrombin Thrombin - pharmacology Time Factors |
| title | Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin |
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