Purification of a Serine Protease of Vibrio parahaemolyticus and Its Characterization
A 50 kDa protease designated as VPP1 was purified from the culture supernatant of a clinical strain of Vibrio parahaemolyticus by ammonium sulfate fractionation, Sephacryl S‐200 HR gel filtration and Fractogel EMD TMAE 650 ion‐exchange chromatography. VPP1 was inhibited by EDTA, EGTA and serine prot...
Gespeichert in:
| Veröffentlicht in: | Microbiology and immunology 2002-01, Vol.46 (4), p.299-303 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 303 |
|---|---|
| container_issue | 4 |
| container_start_page | 299 |
| container_title | Microbiology and immunology |
| container_volume | 46 |
| creator | Ishihara, Masami Kawanishi, Ayako Watanabe, Hirofumi Tomochika, Ken-ichi Miyoshi, Shin-ichi Shinoda, Sumio |
| description | A 50 kDa protease designated as VPP1 was purified from the culture supernatant of a clinical strain of Vibrio parahaemolyticus by ammonium sulfate fractionation, Sephacryl S‐200 HR gel filtration and Fractogel EMD TMAE 650 ion‐exchange chromatography. VPP1 was inhibited by EDTA, EGTA and serine protease inhibitors, suggesting that it is a calcium‐dependent serine protease. N‐terminal amino acid sequence of VPP1 was quite similar to that of V. metschnikovii protease and antibody against VPP1 inhibited the activity of V. metschnikovii protease, suggesting the similarity of the two proteases. It was demonstrated that VPP1 or its related protease widely distribute in not only V. parahaemolyticus but also V. alginolyticus. |
| doi_str_mv | 10.1111/j.1348-0421.2002.tb02699.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71805964</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71805964</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5869-d7d426082a9ba723875e9797233412315c933402cf5c572685d9c86a837c7dc63</originalsourceid><addsrcrecordid>eNqVkFuP0zAQhS0EYsvCX0ARErwl-BLfeGKpaKnUwkqw8GhNHUfrkibFTkTLr8fZRruPCL945PnOmfFB6BXBBUnn7a4grFQ5LikpKMa06LeYCq2L4yM0u289RjPMFM-5wPgCPYtxl1BJVfkUXRCKBRGMzdDN9RB87S30vmuzrs4g--qCb112HbreQXTj43e_Db7LDhDgFty-a069t0PMoK2yVR-z-W3q2D4J_9wZPUdPamiiezHdl-hm8fHb_FO-_rJcza_WueVK6LySVUkFVhT0FiRlSnKnpU4VKwllhFudKkxtzS2XVCheaasEKCatrKxgl-jN2fcQul-Di73Z-2hd00DruiEaSRTmWpT_BIlilFMmE_juDNrQxRhcbQ7B7yGcDMFmTN_szBixGSM2Y_pmSt8ck_jlNGXY7l31IJ3iTsDrCYBooakDtNbHB46lL-JyXPf9mfvtG3f6jxXMZrW5K5NFfrbwsXfHewsIP42QTHLz4_PSfCDlerlYLM2G_QXsKq-A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18325237</pqid></control><display><type>article</type><title>Purification of a Serine Protease of Vibrio parahaemolyticus and Its Characterization</title><source>MEDLINE</source><source>Wiley Journals</source><source>Wiley Free Content</source><source>Freely Accessible Japanese Titles</source><source>Alma/SFX Local Collection</source><creator>Ishihara, Masami ; Kawanishi, Ayako ; Watanabe, Hirofumi ; Tomochika, Ken-ichi ; Miyoshi, Shin-ichi ; Shinoda, Sumio</creator><creatorcontrib>Ishihara, Masami ; Kawanishi, Ayako ; Watanabe, Hirofumi ; Tomochika, Ken-ichi ; Miyoshi, Shin-ichi ; Shinoda, Sumio</creatorcontrib><description>A 50 kDa protease designated as VPP1 was purified from the culture supernatant of a clinical strain of Vibrio parahaemolyticus by ammonium sulfate fractionation, Sephacryl S‐200 HR gel filtration and Fractogel EMD TMAE 650 ion‐exchange chromatography. VPP1 was inhibited by EDTA, EGTA and serine protease inhibitors, suggesting that it is a calcium‐dependent serine protease. N‐terminal amino acid sequence of VPP1 was quite similar to that of V. metschnikovii protease and antibody against VPP1 inhibited the activity of V. metschnikovii protease, suggesting the similarity of the two proteases. It was demonstrated that VPP1 or its related protease widely distribute in not only V. parahaemolyticus but also V. alginolyticus.</description><identifier>ISSN: 0385-5600</identifier><identifier>EISSN: 1348-0421</identifier><identifier>DOI: 10.1111/j.1348-0421.2002.tb02699.x</identifier><identifier>PMID: 12061633</identifier><identifier>CODEN: MIIMDV</identifier><language>eng</language><publisher>Tokyo: Blackwell Publishing Ltd</publisher><subject>Bacteriology ; Biological and medical sciences ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Sequence Analysis, Protein ; Serine Endopeptidases - chemistry ; Serine Endopeptidases - isolation & purification ; Serine Endopeptidases - metabolism ; Serine Endopeptidases - physiology ; serine protease ; Vibrio parahaemolyticus ; Vibrio parahaemolyticus - enzymology ; Vibrio parahaemolyticus - immunology ; Vibrio parahaemolyticus - pathogenicity ; Virulence</subject><ispartof>Microbiology and immunology, 2002-01, Vol.46 (4), p.299-303</ispartof><rights>owned by Center for Academic Publications Japan (Publisher)</rights><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5869-d7d426082a9ba723875e9797233412315c933402cf5c572685d9c86a837c7dc63</citedby><cites>FETCH-LOGICAL-c5869-d7d426082a9ba723875e9797233412315c933402cf5c572685d9c86a837c7dc63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1348-0421.2002.tb02699.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1348-0421.2002.tb02699.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13685044$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12061633$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ishihara, Masami</creatorcontrib><creatorcontrib>Kawanishi, Ayako</creatorcontrib><creatorcontrib>Watanabe, Hirofumi</creatorcontrib><creatorcontrib>Tomochika, Ken-ichi</creatorcontrib><creatorcontrib>Miyoshi, Shin-ichi</creatorcontrib><creatorcontrib>Shinoda, Sumio</creatorcontrib><title>Purification of a Serine Protease of Vibrio parahaemolyticus and Its Characterization</title><title>Microbiology and immunology</title><addtitle>Microbiology and Immunology</addtitle><description>A 50 kDa protease designated as VPP1 was purified from the culture supernatant of a clinical strain of Vibrio parahaemolyticus by ammonium sulfate fractionation, Sephacryl S‐200 HR gel filtration and Fractogel EMD TMAE 650 ion‐exchange chromatography. VPP1 was inhibited by EDTA, EGTA and serine protease inhibitors, suggesting that it is a calcium‐dependent serine protease. N‐terminal amino acid sequence of VPP1 was quite similar to that of V. metschnikovii protease and antibody against VPP1 inhibited the activity of V. metschnikovii protease, suggesting the similarity of the two proteases. It was demonstrated that VPP1 or its related protease widely distribute in not only V. parahaemolyticus but also V. alginolyticus.</description><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Sequence Analysis, Protein</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - isolation & purification</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Serine Endopeptidases - physiology</subject><subject>serine protease</subject><subject>Vibrio parahaemolyticus</subject><subject>Vibrio parahaemolyticus - enzymology</subject><subject>Vibrio parahaemolyticus - immunology</subject><subject>Vibrio parahaemolyticus - pathogenicity</subject><subject>Virulence</subject><issn>0385-5600</issn><issn>1348-0421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkFuP0zAQhS0EYsvCX0ARErwl-BLfeGKpaKnUwkqw8GhNHUfrkibFTkTLr8fZRruPCL945PnOmfFB6BXBBUnn7a4grFQ5LikpKMa06LeYCq2L4yM0u289RjPMFM-5wPgCPYtxl1BJVfkUXRCKBRGMzdDN9RB87S30vmuzrs4g--qCb112HbreQXTj43e_Db7LDhDgFty-a069t0PMoK2yVR-z-W3q2D4J_9wZPUdPamiiezHdl-hm8fHb_FO-_rJcza_WueVK6LySVUkFVhT0FiRlSnKnpU4VKwllhFudKkxtzS2XVCheaasEKCatrKxgl-jN2fcQul-Di73Z-2hd00DruiEaSRTmWpT_BIlilFMmE_juDNrQxRhcbQ7B7yGcDMFmTN_szBixGSM2Y_pmSt8ck_jlNGXY7l31IJ3iTsDrCYBooakDtNbHB46lL-JyXPf9mfvtG3f6jxXMZrW5K5NFfrbwsXfHewsIP42QTHLz4_PSfCDlerlYLM2G_QXsKq-A</recordid><startdate>20020101</startdate><enddate>20020101</enddate><creator>Ishihara, Masami</creator><creator>Kawanishi, Ayako</creator><creator>Watanabe, Hirofumi</creator><creator>Tomochika, Ken-ichi</creator><creator>Miyoshi, Shin-ichi</creator><creator>Shinoda, Sumio</creator><general>Blackwell Publishing Ltd</general><general>Center for Academic Publications Japan</general><scope>BSCLL</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20020101</creationdate><title>Purification of a Serine Protease of Vibrio parahaemolyticus and Its Characterization</title><author>Ishihara, Masami ; Kawanishi, Ayako ; Watanabe, Hirofumi ; Tomochika, Ken-ichi ; Miyoshi, Shin-ichi ; Shinoda, Sumio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5869-d7d426082a9ba723875e9797233412315c933402cf5c572685d9c86a837c7dc63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Sequence Analysis, Protein</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Endopeptidases - isolation & purification</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Serine Endopeptidases - physiology</topic><topic>serine protease</topic><topic>Vibrio parahaemolyticus</topic><topic>Vibrio parahaemolyticus - enzymology</topic><topic>Vibrio parahaemolyticus - immunology</topic><topic>Vibrio parahaemolyticus - pathogenicity</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ishihara, Masami</creatorcontrib><creatorcontrib>Kawanishi, Ayako</creatorcontrib><creatorcontrib>Watanabe, Hirofumi</creatorcontrib><creatorcontrib>Tomochika, Ken-ichi</creatorcontrib><creatorcontrib>Miyoshi, Shin-ichi</creatorcontrib><creatorcontrib>Shinoda, Sumio</creatorcontrib><collection>Istex</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Microbiology and immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ishihara, Masami</au><au>Kawanishi, Ayako</au><au>Watanabe, Hirofumi</au><au>Tomochika, Ken-ichi</au><au>Miyoshi, Shin-ichi</au><au>Shinoda, Sumio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of a Serine Protease of Vibrio parahaemolyticus and Its Characterization</atitle><jtitle>Microbiology and immunology</jtitle><addtitle>Microbiology and Immunology</addtitle><date>2002-01-01</date><risdate>2002</risdate><volume>46</volume><issue>4</issue><spage>299</spage><epage>303</epage><pages>299-303</pages><issn>0385-5600</issn><eissn>1348-0421</eissn><coden>MIIMDV</coden><abstract>A 50 kDa protease designated as VPP1 was purified from the culture supernatant of a clinical strain of Vibrio parahaemolyticus by ammonium sulfate fractionation, Sephacryl S‐200 HR gel filtration and Fractogel EMD TMAE 650 ion‐exchange chromatography. VPP1 was inhibited by EDTA, EGTA and serine protease inhibitors, suggesting that it is a calcium‐dependent serine protease. N‐terminal amino acid sequence of VPP1 was quite similar to that of V. metschnikovii protease and antibody against VPP1 inhibited the activity of V. metschnikovii protease, suggesting the similarity of the two proteases. It was demonstrated that VPP1 or its related protease widely distribute in not only V. parahaemolyticus but also V. alginolyticus.</abstract><cop>Tokyo</cop><pub>Blackwell Publishing Ltd</pub><pmid>12061633</pmid><doi>10.1111/j.1348-0421.2002.tb02699.x</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0385-5600 |
| ispartof | Microbiology and immunology, 2002-01, Vol.46 (4), p.299-303 |
| issn | 0385-5600 1348-0421 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71805964 |
| source | MEDLINE; Wiley Journals; Wiley Free Content; Freely Accessible Japanese Titles; Alma/SFX Local Collection |
| subjects | Bacteriology Biological and medical sciences Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Microbiology Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Sequence Analysis, Protein Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification Serine Endopeptidases - metabolism Serine Endopeptidases - physiology serine protease Vibrio parahaemolyticus Vibrio parahaemolyticus - enzymology Vibrio parahaemolyticus - immunology Vibrio parahaemolyticus - pathogenicity Virulence |
| title | Purification of a Serine Protease of Vibrio parahaemolyticus and Its Characterization |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T04%3A42%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20of%20a%20Serine%20Protease%20of%20Vibrio%20parahaemolyticus%20and%20Its%20Characterization&rft.jtitle=Microbiology%20and%20immunology&rft.au=Ishihara,%20Masami&rft.date=2002-01-01&rft.volume=46&rft.issue=4&rft.spage=299&rft.epage=303&rft.pages=299-303&rft.issn=0385-5600&rft.eissn=1348-0421&rft.coden=MIIMDV&rft_id=info:doi/10.1111/j.1348-0421.2002.tb02699.x&rft_dat=%3Cproquest_cross%3E71805964%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=18325237&rft_id=info:pmid/12061633&rfr_iscdi=true |