Properties of extracellular proteinase—an activator of protein C in blood plasma formed by Aspergillus ochraceus
The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of Aspergillus ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the bas...
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| Veröffentlicht in: | Applied biochemistry and microbiology 2015, Vol.51 (1), p.95-101 |
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| creator | Osmolovskiy, A. A Kreyer, V. G Baranova, N. A Kurakov, A. V Egorov, N. S |
| description | The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of Aspergillus ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the basis of inhibitory analysis, the protein C-activating proteinase from A. ochraceus VKM F-4104D appeared to be a serine proteinase-protein C activator, together with that isolated from the venom of Agkistrodon contortrix contortrix. The isolated enzyme was a nonglycosylated protein with a molecular weight of about 33 kDa, pI 6.0 with an observed optimal activity under a pH of 8.0–9.0 and 37°C. A comparison of the properties of the protein C-activating proteinase formed by A. ochraceus and the enzyme derived from the venom of Agk. contortrix contortrix demonstrated a similarity in their properties; however, proteinase from the micromycete appeared to be in the nonglycosylated state and possessed the ability to hydrolyze the chromogenic plasmin substrate H-D-Val-Leu-Lys-pNA. |
| doi_str_mv | 10.1134/S0003683815010123 |
| format | Article |
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A ; Kreyer, V. G ; Baranova, N. A ; Kurakov, A. V ; Egorov, N. S</creator><creatorcontrib>Osmolovskiy, A. A ; Kreyer, V. G ; Baranova, N. A ; Kurakov, A. V ; Egorov, N. S</creatorcontrib><description>The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of Aspergillus ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the basis of inhibitory analysis, the protein C-activating proteinase from A. ochraceus VKM F-4104D appeared to be a serine proteinase-protein C activator, together with that isolated from the venom of Agkistrodon contortrix contortrix. The isolated enzyme was a nonglycosylated protein with a molecular weight of about 33 kDa, pI 6.0 with an observed optimal activity under a pH of 8.0–9.0 and 37°C. A comparison of the properties of the protein C-activating proteinase formed by A. ochraceus and the enzyme derived from the venom of Agk. contortrix contortrix demonstrated a similarity in their properties; however, proteinase from the micromycete appeared to be in the nonglycosylated state and possessed the ability to hydrolyze the chromogenic plasmin substrate H-D-Val-Leu-Lys-pNA.</description><identifier>ISSN: 0003-6838</identifier><identifier>EISSN: 1608-3024</identifier><identifier>DOI: 10.1134/S0003683815010123</identifier><language>eng</language><publisher>Moscow: Springer-Verlag</publisher><subject>Agkistrodon contortrix ; Agkistrodon contortrix contortrix ; Aspergillus alutaceus ; Aspergillus ochraceus ; Biochemistry ; Biomedical and Life Sciences ; Blood ; blood plasma ; blood proteins ; Cellular biology ; Glycosylation ; Life Sciences ; Medical Microbiology ; Microbiology ; Micromycetes ; molecular weight ; Plasma ; plasmin ; Proteins ; serine ; substrate specificity ; Substrates ; venoms</subject><ispartof>Applied biochemistry and microbiology, 2015, Vol.51 (1), p.95-101</ispartof><rights>Pleiades Publishing, Inc. 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-95c4189cfb3e74767055091260a02b66eaca8ee629e19b37920d8345fa28b70e3</citedby><cites>FETCH-LOGICAL-c373t-95c4189cfb3e74767055091260a02b66eaca8ee629e19b37920d8345fa28b70e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0003683815010123$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0003683815010123$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,4025,27924,27925,27926,41489,42558,51320</link.rule.ids></links><search><creatorcontrib>Osmolovskiy, A. A</creatorcontrib><creatorcontrib>Kreyer, V. G</creatorcontrib><creatorcontrib>Baranova, N. A</creatorcontrib><creatorcontrib>Kurakov, A. V</creatorcontrib><creatorcontrib>Egorov, N. S</creatorcontrib><title>Properties of extracellular proteinase—an activator of protein C in blood plasma formed by Aspergillus ochraceus</title><title>Applied biochemistry and microbiology</title><addtitle>Appl Biochem Microbiol</addtitle><description>The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of Aspergillus ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the basis of inhibitory analysis, the protein C-activating proteinase from A. ochraceus VKM F-4104D appeared to be a serine proteinase-protein C activator, together with that isolated from the venom of Agkistrodon contortrix contortrix. The isolated enzyme was a nonglycosylated protein with a molecular weight of about 33 kDa, pI 6.0 with an observed optimal activity under a pH of 8.0–9.0 and 37°C. A comparison of the properties of the protein C-activating proteinase formed by A. ochraceus and the enzyme derived from the venom of Agk. contortrix contortrix demonstrated a similarity in their properties; however, proteinase from the micromycete appeared to be in the nonglycosylated state and possessed the ability to hydrolyze the chromogenic plasmin substrate H-D-Val-Leu-Lys-pNA.</description><subject>Agkistrodon contortrix</subject><subject>Agkistrodon contortrix contortrix</subject><subject>Aspergillus alutaceus</subject><subject>Aspergillus ochraceus</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Blood</subject><subject>blood plasma</subject><subject>blood proteins</subject><subject>Cellular biology</subject><subject>Glycosylation</subject><subject>Life Sciences</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Micromycetes</subject><subject>molecular weight</subject><subject>Plasma</subject><subject>plasmin</subject><subject>Proteins</subject><subject>serine</subject><subject>substrate specificity</subject><subject>Substrates</subject><subject>venoms</subject><issn>0003-6838</issn><issn>1608-3024</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kc9KxDAQxoMouK4-gCcDXrxUJ0mbJkdZ_AeCgnou0-50rXSbNWlFbz6ET-iTmLIeRMFLhvD9vi-TGcb2BRwLodKTOwBQ2igjMhAgpNpgE6HBJApkuskmo5yM-jbbCeEpXq02dsL8rXcr8n1Dgbua02vvsaK2HVr0fOVdT02HgT7fP7DjWPXNC_bOj-i3yGc8HmXr3JyvWgxL5LXzS5rz8o2fhpi9aGJcTK8ex-gh7LKtGttAe991yh7Oz-5nl8n1zcXV7PQ6qVSu-sRmVSqMrepSUZ7mOocsAyukBgRZak1YoSHS0pKwpcqthLlRaVajNGUOpKbsaJ0bO30eKPTFsgnj37AjN4RC6DQfxyBNRA9_oU9u8F3sLlLKjI9bFSmxpirvQvBUFyvfLNG_FQKKcQvFny1Ej1x7QmS7Bfkfyf-YDtamGl2BC9-E4uFOQtRBaJ2BUV-k6JNC</recordid><startdate>2015</startdate><enddate>2015</enddate><creator>Osmolovskiy, A. 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A</au><au>Kreyer, V. G</au><au>Baranova, N. A</au><au>Kurakov, A. V</au><au>Egorov, N. S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Properties of extracellular proteinase—an activator of protein C in blood plasma formed by Aspergillus ochraceus</atitle><jtitle>Applied biochemistry and microbiology</jtitle><stitle>Appl Biochem Microbiol</stitle><date>2015</date><risdate>2015</risdate><volume>51</volume><issue>1</issue><spage>95</spage><epage>101</epage><pages>95-101</pages><issn>0003-6838</issn><eissn>1608-3024</eissn><abstract>The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of Aspergillus ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the basis of inhibitory analysis, the protein C-activating proteinase from A. ochraceus VKM F-4104D appeared to be a serine proteinase-protein C activator, together with that isolated from the venom of Agkistrodon contortrix contortrix. The isolated enzyme was a nonglycosylated protein with a molecular weight of about 33 kDa, pI 6.0 with an observed optimal activity under a pH of 8.0–9.0 and 37°C. A comparison of the properties of the protein C-activating proteinase formed by A. ochraceus and the enzyme derived from the venom of Agk. contortrix contortrix demonstrated a similarity in their properties; however, proteinase from the micromycete appeared to be in the nonglycosylated state and possessed the ability to hydrolyze the chromogenic plasmin substrate H-D-Val-Leu-Lys-pNA.</abstract><cop>Moscow</cop><pub>Springer-Verlag</pub><doi>10.1134/S0003683815010123</doi><tpages>7</tpages></addata></record> |
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| subjects | Agkistrodon contortrix Agkistrodon contortrix contortrix Aspergillus alutaceus Aspergillus ochraceus Biochemistry Biomedical and Life Sciences Blood blood plasma blood proteins Cellular biology Glycosylation Life Sciences Medical Microbiology Microbiology Micromycetes molecular weight Plasma plasmin Proteins serine substrate specificity Substrates venoms |
| title | Properties of extracellular proteinase—an activator of protein C in blood plasma formed by Aspergillus ochraceus |
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