Partial purification of factors XI and XIa: A comparison of their molecular size and structure

Factors XI and XIa have been purified by using affinity chromatography of plasma or contact product on heparin coupled to Sepharose. Further purification was achieved by chromatography on hydroxylapatite. Both forms of the protein co-chromatographed on Sephadex G-150 and Biogel P-300 and had identic...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Thrombosis research 1975-11, Vol.7 (5), p.717-728
Hauptverfasser:	Connellan, J.M., Castaldi, P.A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Chromatography, Affinity Dithiothreitol - pharmacology Edetic Acid - pharmacology Electrophoresis, Disc Electrophoresis, Polyacrylamide Gel Factor XI - analysis Factor XI - isolation & purification Factor XI - metabolism Humans Imidazoles - pharmacology Molecular Weight
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

container_end_page	728
container_issue	5
container_start_page	717
container_title	Thrombosis research
container_volume	7
creator	Connellan, J.M. Castaldi, P.A.
description	Factors XI and XIa have been purified by using affinity chromatography of plasma or contact product on heparin coupled to Sepharose. Further purification was achieved by chromatography on hydroxylapatite. Both forms of the protein co-chromatographed on Sephadex G-150 and Biogel P-300 and had identical mobility on gradient polyacrylamide electrophoresis; their molecular weight was estimated at approximately 230,000. A slight difference in electrophoretic mobility was observed when the samples were electrophoresed on polyacrylamide in 8M urea. Chemical modification studies show that both forms are inactivated by dithiothreitol and N-acetylimidazole but not by 5,5′ dithio-bis-(2-nitrobenzoic acid), iodoacetamide or EDTA.
doi_str_mv	10.1016/0049-3848(75)90197-8
format	Article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83187431</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0049384875901978</els_id><sourcerecordid>83187431</sourcerecordid><originalsourceid>FETCH-LOGICAL-c271t-e5a609b22d7fd2a1929117dd87a691649edbbf2376f34beb17861720f3b7bc4d3</originalsourceid><addsrcrecordid>eNp9kMFO3DAURS1EgWHoH8zCKwSLUD87E8ddIKFRaZGQ2kUrdYXl2M-qUTKe2g5S-fpmCGLJ6i3uuVd6h5AVsCtg0HxirFaVaOv2Qq4vFQMlq_aALKCVquK15Idk8YackNOcHxkDCWp9TI5aEILLBXn4YVIJpqe7MQUfrCkhbmn01BtbYsr09x01Wzcd85neUBuHnUkhz0z5gyHRIfZox94kmsMzvtC5pNGWMeEZ-eBNn_Hj612SX7dffm6-Vfffv95tbu4ryyWUCtemYarj3EnvuAHFFYB0rpWmUdDUCl3XeS5k40XdYQeybUBy5kUnO1s7sSTn8-4uxb8j5qKHkC32vdliHLNuxWSlFjCB9QzaFHNO6PUuhcGkfxqY3lvVe2V6r0zLtX6xOrWXZPW6P3YDurfSrHGKr-cYpx-fAiadbcCtRRcS2qJdDO_v_wc2M4Z_</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83187431</pqid></control><display><type>article</type><title>Partial purification of factors XI and XIa: A comparison of their molecular size and structure</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Connellan, J.M. ; Castaldi, P.A.</creator><creatorcontrib>Connellan, J.M. ; Castaldi, P.A.</creatorcontrib><description>Factors XI and XIa have been purified by using affinity chromatography of plasma or contact product on heparin coupled to Sepharose. Further purification was achieved by chromatography on hydroxylapatite. Both forms of the protein co-chromatographed on Sephadex G-150 and Biogel P-300 and had identical mobility on gradient polyacrylamide electrophoresis; their molecular weight was estimated at approximately 230,000. A slight difference in electrophoretic mobility was observed when the samples were electrophoresed on polyacrylamide in 8M urea. Chemical modification studies show that both forms are inactivated by dithiothreitol and N-acetylimidazole but not by 5,5′ dithio-bis-(2-nitrobenzoic acid), iodoacetamide or EDTA.</description><identifier>ISSN: 0049-3848</identifier><identifier>EISSN: 1879-2472</identifier><identifier>DOI: 10.1016/0049-3848(75)90197-8</identifier><identifier>PMID: 813327</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Chromatography, Affinity ; Dithiothreitol - pharmacology ; Edetic Acid - pharmacology ; Electrophoresis, Disc ; Electrophoresis, Polyacrylamide Gel ; Factor XI - analysis ; Factor XI - isolation & purification ; Factor XI - metabolism ; Humans ; Imidazoles - pharmacology ; Molecular Weight</subject><ispartof>Thrombosis research, 1975-11, Vol.7 (5), p.717-728</ispartof><rights>1975</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c271t-e5a609b22d7fd2a1929117dd87a691649edbbf2376f34beb17861720f3b7bc4d3</citedby><cites>FETCH-LOGICAL-c271t-e5a609b22d7fd2a1929117dd87a691649edbbf2376f34beb17861720f3b7bc4d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0049-3848(75)90197-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27911,27912,45982</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/813327$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Connellan, J.M.</creatorcontrib><creatorcontrib>Castaldi, P.A.</creatorcontrib><title>Partial purification of factors XI and XIa: A comparison of their molecular size and structure</title><title>Thrombosis research</title><addtitle>Thromb Res</addtitle><description>Factors XI and XIa have been purified by using affinity chromatography of plasma or contact product on heparin coupled to Sepharose. Further purification was achieved by chromatography on hydroxylapatite. Both forms of the protein co-chromatographed on Sephadex G-150 and Biogel P-300 and had identical mobility on gradient polyacrylamide electrophoresis; their molecular weight was estimated at approximately 230,000. A slight difference in electrophoretic mobility was observed when the samples were electrophoresed on polyacrylamide in 8M urea. Chemical modification studies show that both forms are inactivated by dithiothreitol and N-acetylimidazole but not by 5,5′ dithio-bis-(2-nitrobenzoic acid), iodoacetamide or EDTA.</description><subject>Chromatography, Affinity</subject><subject>Dithiothreitol - pharmacology</subject><subject>Edetic Acid - pharmacology</subject><subject>Electrophoresis, Disc</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Factor XI - analysis</subject><subject>Factor XI - isolation & purification</subject><subject>Factor XI - metabolism</subject><subject>Humans</subject><subject>Imidazoles - pharmacology</subject><subject>Molecular Weight</subject><issn>0049-3848</issn><issn>1879-2472</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFO3DAURS1EgWHoH8zCKwSLUD87E8ddIKFRaZGQ2kUrdYXl2M-qUTKe2g5S-fpmCGLJ6i3uuVd6h5AVsCtg0HxirFaVaOv2Qq4vFQMlq_aALKCVquK15Idk8YackNOcHxkDCWp9TI5aEILLBXn4YVIJpqe7MQUfrCkhbmn01BtbYsr09x01Wzcd85neUBuHnUkhz0z5gyHRIfZox94kmsMzvtC5pNGWMeEZ-eBNn_Hj612SX7dffm6-Vfffv95tbu4ryyWUCtemYarj3EnvuAHFFYB0rpWmUdDUCl3XeS5k40XdYQeybUBy5kUnO1s7sSTn8-4uxb8j5qKHkC32vdliHLNuxWSlFjCB9QzaFHNO6PUuhcGkfxqY3lvVe2V6r0zLtX6xOrWXZPW6P3YDurfSrHGKr-cYpx-fAiadbcCtRRcS2qJdDO_v_wc2M4Z_</recordid><startdate>197511</startdate><enddate>197511</enddate><creator>Connellan, J.M.</creator><creator>Castaldi, P.A.</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>197511</creationdate><title>Partial purification of factors XI and XIa: A comparison of their molecular size and structure</title><author>Connellan, J.M. ; Castaldi, P.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c271t-e5a609b22d7fd2a1929117dd87a691649edbbf2376f34beb17861720f3b7bc4d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Chromatography, Affinity</topic><topic>Dithiothreitol - pharmacology</topic><topic>Edetic Acid - pharmacology</topic><topic>Electrophoresis, Disc</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Factor XI - analysis</topic><topic>Factor XI - isolation & purification</topic><topic>Factor XI - metabolism</topic><topic>Humans</topic><topic>Imidazoles - pharmacology</topic><topic>Molecular Weight</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Connellan, J.M.</creatorcontrib><creatorcontrib>Castaldi, P.A.</creatorcontrib><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>Thrombosis research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Connellan, J.M.</au><au>Castaldi, P.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Partial purification of factors XI and XIa: A comparison of their molecular size and structure</atitle><jtitle>Thrombosis research</jtitle><addtitle>Thromb Res</addtitle><date>1975-11</date><risdate>1975</risdate><volume>7</volume><issue>5</issue><spage>717</spage><epage>728</epage><pages>717-728</pages><issn>0049-3848</issn><eissn>1879-2472</eissn><abstract>Factors XI and XIa have been purified by using affinity chromatography of plasma or contact product on heparin coupled to Sepharose. Further purification was achieved by chromatography on hydroxylapatite. Both forms of the protein co-chromatographed on Sephadex G-150 and Biogel P-300 and had identical mobility on gradient polyacrylamide electrophoresis; their molecular weight was estimated at approximately 230,000. A slight difference in electrophoretic mobility was observed when the samples were electrophoresed on polyacrylamide in 8M urea. Chemical modification studies show that both forms are inactivated by dithiothreitol and N-acetylimidazole but not by 5,5′ dithio-bis-(2-nitrobenzoic acid), iodoacetamide or EDTA.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>813327</pmid><doi>10.1016/0049-3848(75)90197-8</doi><tpages>12</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0049-3848
ispartof	Thrombosis research, 1975-11, Vol.7 (5), p.717-728
issn	0049-3848 1879-2472
language	eng
recordid	cdi_proquest_miscellaneous_83187431
source	MEDLINE; ScienceDirect Journals (5 years ago - present)
subjects	Chromatography, Affinity Dithiothreitol - pharmacology Edetic Acid - pharmacology Electrophoresis, Disc Electrophoresis, Polyacrylamide Gel Factor XI - analysis Factor XI - isolation & purification Factor XI - metabolism Humans Imidazoles - pharmacology Molecular Weight
title	Partial purification of factors XI and XIa: A comparison of their molecular size and structure
url	https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T12%3A40%3A38IST&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=Partial%20purification%20of%20factors%20XI%20and%20XIa:%20A%20comparison%20of%20their%20molecular%20size%20and%20structure&rft.jtitle=Thrombosis%20research&rft.au=Connellan,%20J.M.&rft.date=1975-11&rft.volume=7&rft.issue=5&rft.spage=717&rft.epage=728&rft.pages=717-728&rft.issn=0049-3848&rft.eissn=1879-2472&rft_id=info:doi/10.1016/0049-3848(75)90197-8&rft_dat=%3Cproquest_cross%3E83187431%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=83187431&rft_id=info:pmid/813327&rft_els_id=0049384875901978&rfr_iscdi=true