Purification and characterization of putative endothelin converting enzyme in bovine adrenal medulla: Evidence for a cathepsin D-like enzyme
A specific and sensitive assay has been established for measurement of endothelin converting activity in a tissue extract. This assay is based on measuring endothelin-1 generated from big endothelin-1 by endothelin converting enzyme (ECE) with radioimmunoassay using an endothelin C-terminal specific...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1990-05, Vol.168 (3), p.1230-1236 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Sawamura, Tatsuya Kimura, Sadao Shinmi, Osamu Sugita, Yoshiki Yanagisawa, Masashi Goto, Katsutoshi Masaki, Tomoh |
| description | A specific and sensitive assay has been established for measurement of endothelin converting activity in a tissue extract. This assay is based on measuring endothelin-1 generated from big endothelin-1 by endothelin converting enzyme (ECE) with radioimmunoassay using an endothelin C-terminal specific antibody. By using this assay, we purified and characterized ECE in bovineadrenomedullary chromaffin granules. ECE was purified over 3,000 times by a combination of DEAE, hydrophobic and gel filtration chromatography. A molecular weight of ECE was estimated to be approximately 30,000 by gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that ECE had three major components with estimated molecular weights of 45,000, 30,000 and 15,000 like bovine spleen cathepsin D. ECE had a pH optimum at 3.5 and was inhibited by pepstatin. These results strongly suggest that ECE is a cathepsin D-like aspartic protease. |
| doi_str_mv | 10.1016/0006-291X(90)91160-T |
| format | Article |
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This assay is based on measuring endothelin-1 generated from big endothelin-1 by endothelin converting enzyme (ECE) with radioimmunoassay using an endothelin C-terminal specific antibody. By using this assay, we purified and characterized ECE in bovineadrenomedullary chromaffin granules. ECE was purified over 3,000 times by a combination of DEAE, hydrophobic and gel filtration chromatography. A molecular weight of ECE was estimated to be approximately 30,000 by gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that ECE had three major components with estimated molecular weights of 45,000, 30,000 and 15,000 like bovine spleen cathepsin D. ECE had a pH optimum at 3.5 and was inhibited by pepstatin. These results strongly suggest that ECE is a cathepsin D-like aspartic protease.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(90)91160-T</identifier><identifier>PMID: 2189405</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Adrenal Medulla - enzymology ; Analytical, structural and metabolic biochemistry ; Animals ; Aspartic Acid Endopeptidases ; Biological and medical sciences ; Cathepsin D - metabolism ; Cattle ; Chromaffin Granules - enzymology ; Chromatography, Gel ; Chromatography, Ion Exchange ; Electrophoresis, Polyacrylamide Gel ; Endopeptidases - isolation & purification ; Endopeptidases - metabolism ; Endothelin-Converting Enzymes ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Hydrolases ; Metalloendopeptidases ; Molecular Weight ; Peptide Hydrolases ; Radioimmunoassay</subject><ispartof>Biochemical and biophysical research communications, 1990-05, Vol.168 (3), p.1230-1236</ispartof><rights>1990</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c453t-2dd4d084f681e6bcdfb10052165b254c7963e4de42055c627585678eb1f645703</citedby><cites>FETCH-LOGICAL-c453t-2dd4d084f681e6bcdfb10052165b254c7963e4de42055c627585678eb1f645703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(90)91160-T$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19545543$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2189405$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sawamura, Tatsuya</creatorcontrib><creatorcontrib>Kimura, Sadao</creatorcontrib><creatorcontrib>Shinmi, Osamu</creatorcontrib><creatorcontrib>Sugita, Yoshiki</creatorcontrib><creatorcontrib>Yanagisawa, Masashi</creatorcontrib><creatorcontrib>Goto, Katsutoshi</creatorcontrib><creatorcontrib>Masaki, Tomoh</creatorcontrib><title>Purification and characterization of putative endothelin converting enzyme in bovine adrenal medulla: Evidence for a cathepsin D-like enzyme</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>A specific and sensitive assay has been established for measurement of endothelin converting activity in a tissue extract. This assay is based on measuring endothelin-1 generated from big endothelin-1 by endothelin converting enzyme (ECE) with radioimmunoassay using an endothelin C-terminal specific antibody. By using this assay, we purified and characterized ECE in bovineadrenomedullary chromaffin granules. ECE was purified over 3,000 times by a combination of DEAE, hydrophobic and gel filtration chromatography. A molecular weight of ECE was estimated to be approximately 30,000 by gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that ECE had three major components with estimated molecular weights of 45,000, 30,000 and 15,000 like bovine spleen cathepsin D. ECE had a pH optimum at 3.5 and was inhibited by pepstatin. These results strongly suggest that ECE is a cathepsin D-like aspartic protease.</description><subject>Adrenal Medulla - enzymology</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Aspartic Acid Endopeptidases</subject><subject>Biological and medical sciences</subject><subject>Cathepsin D - metabolism</subject><subject>Cattle</subject><subject>Chromaffin Granules - enzymology</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endopeptidases - isolation & purification</subject><subject>Endopeptidases - metabolism</subject><subject>Endothelin-Converting Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases</subject><subject>Metalloendopeptidases</subject><subject>Molecular Weight</subject><subject>Peptide Hydrolases</subject><subject>Radioimmunoassay</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc-KFDEQxoMo67j6Bgq5KHporfQk6Y4HQdb1DyzoYQRvIZ1UO9GeZEy6G3afwYc27TTrzVNC1fd9VfyKkMcMXjJg8hUAyKpW7NtzBS8UYxKq3R2yYaCgqhnwu2RzK7lPHuT8A4AxLtUZOatZqziIDfn9ZUq-99aMPgZqgqN2b5KxIyZ_cyrGnh6nsfxnpBhcHPc4-EBtDDOm0YfvpXpzfUBail2cfUBqXMJgBnpANw2DeU0vZ-8wWKR9TNTQMm6Px1wM76rB_8Q14SG515sh46P1PSdf31_uLj5WV58_fLp4e1VZLrZjVTvHHbS8ly1D2VnXdwxA1EyKrhbcNkpukTvkNQhhZd2IVsimxY71kosGtufk2Sn3mOKvCfOoDz5bLJsGjFPWjWoBVLstQn4S2hRzTtjrY_IHk641A70cQS-E9UJYK9B_j6B3xfZkzZ-6guDWtFIv_adr32Rrhj6ZYH3-l60EF4Iv49-cdFhgzB6TztYvGJ1PaEftov__In8AGaOllg</recordid><startdate>19900516</startdate><enddate>19900516</enddate><creator>Sawamura, Tatsuya</creator><creator>Kimura, Sadao</creator><creator>Shinmi, Osamu</creator><creator>Sugita, Yoshiki</creator><creator>Yanagisawa, Masashi</creator><creator>Goto, Katsutoshi</creator><creator>Masaki, Tomoh</creator><general>Elsevier Inc</general><general>Elsevier</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>19900516</creationdate><title>Purification and characterization of putative endothelin converting enzyme in bovine adrenal medulla: Evidence for a cathepsin D-like enzyme</title><author>Sawamura, Tatsuya ; Kimura, Sadao ; Shinmi, Osamu ; Sugita, Yoshiki ; Yanagisawa, Masashi ; Goto, Katsutoshi ; Masaki, Tomoh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c453t-2dd4d084f681e6bcdfb10052165b254c7963e4de42055c627585678eb1f645703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Adrenal Medulla - enzymology</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Aspartic Acid Endopeptidases</topic><topic>Biological and medical sciences</topic><topic>Cathepsin D - metabolism</topic><topic>Cattle</topic><topic>Chromaffin Granules - enzymology</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endopeptidases - isolation & purification</topic><topic>Endopeptidases - metabolism</topic><topic>Endothelin-Converting Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolases</topic><topic>Metalloendopeptidases</topic><topic>Molecular Weight</topic><topic>Peptide Hydrolases</topic><topic>Radioimmunoassay</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sawamura, Tatsuya</creatorcontrib><creatorcontrib>Kimura, Sadao</creatorcontrib><creatorcontrib>Shinmi, Osamu</creatorcontrib><creatorcontrib>Sugita, Yoshiki</creatorcontrib><creatorcontrib>Yanagisawa, Masashi</creatorcontrib><creatorcontrib>Goto, Katsutoshi</creatorcontrib><creatorcontrib>Masaki, Tomoh</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sawamura, Tatsuya</au><au>Kimura, Sadao</au><au>Shinmi, Osamu</au><au>Sugita, Yoshiki</au><au>Yanagisawa, Masashi</au><au>Goto, Katsutoshi</au><au>Masaki, Tomoh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of putative endothelin converting enzyme in bovine adrenal medulla: Evidence for a cathepsin D-like enzyme</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1990-05-16</date><risdate>1990</risdate><volume>168</volume><issue>3</issue><spage>1230</spage><epage>1236</epage><pages>1230-1236</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>A specific and sensitive assay has been established for measurement of endothelin converting activity in a tissue extract. This assay is based on measuring endothelin-1 generated from big endothelin-1 by endothelin converting enzyme (ECE) with radioimmunoassay using an endothelin C-terminal specific antibody. By using this assay, we purified and characterized ECE in bovineadrenomedullary chromaffin granules. ECE was purified over 3,000 times by a combination of DEAE, hydrophobic and gel filtration chromatography. A molecular weight of ECE was estimated to be approximately 30,000 by gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that ECE had three major components with estimated molecular weights of 45,000, 30,000 and 15,000 like bovine spleen cathepsin D. ECE had a pH optimum at 3.5 and was inhibited by pepstatin. These results strongly suggest that ECE is a cathepsin D-like aspartic protease.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2189405</pmid><doi>10.1016/0006-291X(90)91160-T</doi><tpages>7</tpages></addata></record> |
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| subjects | Adrenal Medulla - enzymology Analytical, structural and metabolic biochemistry Animals Aspartic Acid Endopeptidases Biological and medical sciences Cathepsin D - metabolism Cattle Chromaffin Granules - enzymology Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Endopeptidases - isolation & purification Endopeptidases - metabolism Endothelin-Converting Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases Metalloendopeptidases Molecular Weight Peptide Hydrolases Radioimmunoassay |
| title | Purification and characterization of putative endothelin converting enzyme in bovine adrenal medulla: Evidence for a cathepsin D-like enzyme |
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