Purification and characterization of kininogens from sheep plasma
High molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK) have been purified from sheep (Avis Arias) plasma in three steps involving ammonium sulphate precipitation, column chromatography on Sephacryl-300HR and ion exchange chromatography on DEAE cellulose. HMWK gave a single...
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| Veröffentlicht in: | The Protein Journal 2005-02, Vol.24 (2), p.95-102 |
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| creator | Baba, Shahid P Zehra, Sadaf Bano, Bilqees |
| description | High molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK) have been purified from sheep (Avis Arias) plasma in three steps involving ammonium sulphate precipitation, column chromatography on Sephacryl-300HR and ion exchange chromatography on DEAE cellulose. HMWK gave a single band on native and SDS-PAGE with a molecular weight corresponding to 280 kDa. Under reducing conditions purified HMWK was again resolved to a single band with molecular weight corresponding to 140 kDa indicative of its dimeric nature. LMWK was resolved into two isoforms named as LMWK1 and LMWK2, with an apparent molecular weight of 68 kDa. The yield of HMWK, LMWK1 and 2 was about 8.1, 5.63 and 10.65 respectively. HMWK, LMWK1 and 2 strongly inhibited activities of ficin and papain but not of trypsin, chymotrypsin and bromelain. Ki values estimated for HMWK with papain and ficin was 0.8 and 0.6 nM respectively. Ki values estimated for LMWK1 and 2 with papain were 2.40 and 2.00 nM respectively. Binding of HMWK, LMWK1 and 2 to activated papain were accompanied by pronounced changes in secondary and tertiary structure that are compatible with perturbations of environment of aromatic residues. |
| doi_str_mv | 10.1007/s10930-004-1516-6 |
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HMWK gave a single band on native and SDS-PAGE with a molecular weight corresponding to 280 kDa. Under reducing conditions purified HMWK was again resolved to a single band with molecular weight corresponding to 140 kDa indicative of its dimeric nature. LMWK was resolved into two isoforms named as LMWK1 and LMWK2, with an apparent molecular weight of 68 kDa. The yield of HMWK, LMWK1 and 2 was about 8.1, 5.63 and 10.65 respectively. HMWK, LMWK1 and 2 strongly inhibited activities of ficin and papain but not of trypsin, chymotrypsin and bromelain. Ki values estimated for HMWK with papain and ficin was 0.8 and 0.6 nM respectively. Ki values estimated for LMWK1 and 2 with papain were 2.40 and 2.00 nM respectively. Binding of HMWK, LMWK1 and 2 to activated papain were accompanied by pronounced changes in secondary and tertiary structure that are compatible with perturbations of environment of aromatic residues.</description><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1875-8355</identifier><identifier>EISSN: 1573-4943</identifier><identifier>DOI: 10.1007/s10930-004-1516-6</identifier><identifier>PMID: 16003951</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Ammonium ; Animals ; Cellulose ; Chromatography ; Chromatography, Gel ; Chromatography, Ion Exchange ; Circular Dichroism ; Electrophoresis, Polyacrylamide Gel ; Hydrogen-Ion Concentration ; Kinetics ; Kininogens - blood ; Kininogens - isolation & purification ; Molecular Weight ; Oxidation-Reduction ; Proteins ; Sheep ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Temperature</subject><ispartof>The Protein Journal, 2005-02, Vol.24 (2), p.95-102</ispartof><rights>Springer Science+Business Media, Inc. 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c326t-aa4e6eba9ce3f4d673216b5c826cf477ba2f6e28cc64ea03967e2b25942a78b93</citedby><cites>FETCH-LOGICAL-c326t-aa4e6eba9ce3f4d673216b5c826cf477ba2f6e28cc64ea03967e2b25942a78b93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16003951$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baba, Shahid P</creatorcontrib><creatorcontrib>Zehra, Sadaf</creatorcontrib><creatorcontrib>Bano, Bilqees</creatorcontrib><title>Purification and characterization of kininogens from sheep plasma</title><title>The Protein Journal</title><addtitle>Protein J</addtitle><description>High molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK) have been purified from sheep (Avis Arias) plasma in three steps involving ammonium sulphate precipitation, column chromatography on Sephacryl-300HR and ion exchange chromatography on DEAE cellulose. HMWK gave a single band on native and SDS-PAGE with a molecular weight corresponding to 280 kDa. Under reducing conditions purified HMWK was again resolved to a single band with molecular weight corresponding to 140 kDa indicative of its dimeric nature. LMWK was resolved into two isoforms named as LMWK1 and LMWK2, with an apparent molecular weight of 68 kDa. The yield of HMWK, LMWK1 and 2 was about 8.1, 5.63 and 10.65 respectively. HMWK, LMWK1 and 2 strongly inhibited activities of ficin and papain but not of trypsin, chymotrypsin and bromelain. Ki values estimated for HMWK with papain and ficin was 0.8 and 0.6 nM respectively. Ki values estimated for LMWK1 and 2 with papain were 2.40 and 2.00 nM respectively. Binding of HMWK, LMWK1 and 2 to activated papain were accompanied by pronounced changes in secondary and tertiary structure that are compatible with perturbations of environment of aromatic residues.</description><subject>Ammonium</subject><subject>Animals</subject><subject>Cellulose</subject><subject>Chromatography</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Circular Dichroism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Kininogens - blood</subject><subject>Kininogens - isolation & purification</subject><subject>Molecular Weight</subject><subject>Oxidation-Reduction</subject><subject>Proteins</subject><subject>Sheep</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Temperature</subject><issn>1572-3887</issn><issn>1875-8355</issn><issn>1573-4943</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkMtKAzEUhoMotlYfwI0MLtxFT5LJZZaleIOCLnQdMmliU-dmMrPQp3fKFARX53D4zs_Ph9AlgVsCIO8SgYIBBsgx4URgcYTmREmOFeP8eNy5pJgpJWfoLKUdAFWFpKdoRgQAKziZo-XrEIMP1vShbTLTbDK7NdHY3sXwMx1bn32GJjTth2tS5mNbZ2nrXJd1lUm1OUcn3lTJXRzmAr0_3L-tnvD65fF5tVxjy6josTG5E640hXXM5xshGSWi5FZRYX0uZWmoF44qa0XuzNhOSEdLyoucGqnKgi3QzZTbxfZrcKnXdUjWVZVpXDskLRQQECBG8PofuGuH2IzdtOQSZM4UjBCZIBvblKLzuouhNvFbE9B7uXqSq0e5ei9X74OvDsFDWbvN38fBJvsFLJV0mg</recordid><startdate>200502</startdate><enddate>200502</enddate><creator>Baba, Shahid P</creator><creator>Zehra, Sadaf</creator><creator>Bano, Bilqees</creator><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7TK</scope><scope>7TM</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200502</creationdate><title>Purification and characterization of kininogens from sheep plasma</title><author>Baba, Shahid P ; Zehra, Sadaf ; Bano, Bilqees</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c326t-aa4e6eba9ce3f4d673216b5c826cf477ba2f6e28cc64ea03967e2b25942a78b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Ammonium</topic><topic>Animals</topic><topic>Cellulose</topic><topic>Chromatography</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Circular Dichroism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Kininogens - blood</topic><topic>Kininogens - isolation & purification</topic><topic>Molecular Weight</topic><topic>Oxidation-Reduction</topic><topic>Proteins</topic><topic>Sheep</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baba, Shahid P</creatorcontrib><creatorcontrib>Zehra, Sadaf</creatorcontrib><creatorcontrib>Bano, Bilqees</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Protein Journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Baba, Shahid P</au><au>Zehra, Sadaf</au><au>Bano, Bilqees</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of kininogens from sheep plasma</atitle><jtitle>The Protein Journal</jtitle><addtitle>Protein J</addtitle><date>2005-02</date><risdate>2005</risdate><volume>24</volume><issue>2</issue><spage>95</spage><epage>102</epage><pages>95-102</pages><issn>1572-3887</issn><eissn>1875-8355</eissn><eissn>1573-4943</eissn><abstract>High molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK) have been purified from sheep (Avis Arias) plasma in three steps involving ammonium sulphate precipitation, column chromatography on Sephacryl-300HR and ion exchange chromatography on DEAE cellulose. HMWK gave a single band on native and SDS-PAGE with a molecular weight corresponding to 280 kDa. Under reducing conditions purified HMWK was again resolved to a single band with molecular weight corresponding to 140 kDa indicative of its dimeric nature. LMWK was resolved into two isoforms named as LMWK1 and LMWK2, with an apparent molecular weight of 68 kDa. The yield of HMWK, LMWK1 and 2 was about 8.1, 5.63 and 10.65 respectively. HMWK, LMWK1 and 2 strongly inhibited activities of ficin and papain but not of trypsin, chymotrypsin and bromelain. Ki values estimated for HMWK with papain and ficin was 0.8 and 0.6 nM respectively. Ki values estimated for LMWK1 and 2 with papain were 2.40 and 2.00 nM respectively. Binding of HMWK, LMWK1 and 2 to activated papain were accompanied by pronounced changes in secondary and tertiary structure that are compatible with perturbations of environment of aromatic residues.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>16003951</pmid><doi>10.1007/s10930-004-1516-6</doi><tpages>8</tpages></addata></record> |
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| subjects | Ammonium Animals Cellulose Chromatography Chromatography, Gel Chromatography, Ion Exchange Circular Dichroism Electrophoresis, Polyacrylamide Gel Hydrogen-Ion Concentration Kinetics Kininogens - blood Kininogens - isolation & purification Molecular Weight Oxidation-Reduction Proteins Sheep Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Temperature |
| title | Purification and characterization of kininogens from sheep plasma |
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