Content and functional activity of von Willebrand factor in apheresis plasma
Identifieur interne : 000047 ( Istex/Corpus ); précédent : 000046; suivant : 000048Content and functional activity of von Willebrand factor in apheresis plasma
Auteurs : T. Burnouf ; C. Caron ; T. Burkhardt ; J. GoudemandSource :
- Vox Sanguinis [ 0042-9007 ] ; 2004-07.
English descriptors
- Teeft :
- Apheresis, Apheresis plasma, Apheresis plasmas, Apheresis procedures, Assay, Blackwell publishing, Blood group, Burnouf, Collagen binding activity, Cryoprecipitate, Donation, Factor viii, Functional activity, Greater number, Largest multimers, Lter core, Mers, Multimeric structure, Multimers, Normal plasma, Normal plasma pools, Npps, Plasma, Plasma donations, Plasma units, Platelet, Reference plasma, Respective pools, Sanguinis, Secondary haemostasis, Source plasma, Thromb, Thromb haemost, Transfusion, Viii, Willebrand, Willebrand disease, Willebrand factor.
Abstract
Background and Objectives Von Willebrand Factor (VWF) is a complex high‐molecular‐weight (HMW) plasma glycoprotein playing a critical role in primary and secondary haemostasis. Owing to its multimeric structure and sensitivity to proteolysis, VWF can be used as a marker of the impact of collection procedures on the characteristics of plasma for transfusion and for fractionation. We studied VWF content, functional activity and HMW multimers in plasmas collected by five different automated apheresis collection procedures. Materials and Methods Five series of 30 plasma units were obtained from volunteer donors at two collection sites using Haemonetics PCS2 machines with Revision (Rev) F, Rev G, high‐separation core (HSC), or filter core (FC) procedures, or Baxter‐Fenwall Autopheresis‐C (Auto‐C). VWF antigen (VWF:Ag), ristocetin cofactor (VWF:RCo) activity and HMW multimers were first determined in 10 randomly selected plasma donations collected with Rev G, HSC, FC and Auto‐C procedures. Then, the same analyses and the collagen binding (VWF:CB) activity were determined in the pools of 30 donations from each of the five procedures and compared with two normal plasma pools (NPP1 and NPP2). A reference plasma (RP) was used to calibrate each assay. Results There were a greater number of group O individuals in the Rev F, Rev G and FC donors than in the HSC and Auto‐C donors. The mean VWF:Ag level was > 100 IU/dl, VWF:RCo activity was > 90 U/dl, the VWF:RCo/Ag ratio was close to 1, and the percentage of 11–15 mers was above 100% of RP in the 10 individual plasma units from Rev G, HSC, FC, and Auto‐C and in their respective pools. The mean percentage of multimers > 15 mers, relative to RP, was significantly less in Rev G plasmas (48 ± 17%; range 32–91%), compared with Auto‐C, HSC and FC plasmas (P = 0·0211; 0·0257; and 0·0376, respectively). The VWF:CB activity of the 30‐donation pools was 61 and 60 U/dl in Auto C and HSC, 50 U/dl in Rev F and FC, and 43 U/dl in the Rev G pool. The VWF:CB/Ag ratio was 0·54 (Auto‐C), 0·49 (HSC), 0·46 (Rev F), 0·45 (FC) and 0·37 (Rev G), compared with 0·81and 0·92 in NPPs. The percentage of VWF multimers of 11–15 mers in apheresis plasma and NPP was normal. VWF multimers > 15 mers ranged from 38 to 64% of that of RP plasma, and was 111 and 112% in NPPs. Conclusions The VWF:Ag, VWF:RCo activity and 11–15 mer VWF multimers were well preserved in all plasma units from each of the five apheresis procedures. The VWF:CB activity and the percentage of multimers > 15 mers in apheresis plasma was less than in normal plasma pools and differed slightly among procedures.
Url:
DOI: 10.1111/j.1423-0410.2004.00535.x
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ISTEX:D32E13F98B080996EE2C1EC4A23A9B3BA6290E7DLe document en format XML
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Burnouf</name><affiliation><mods:affiliation>Human Plasma Product Services, Lille, France</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: tburnou@attglobal.net</mods:affiliation></affiliation></author><author><name sortKey="Caron, C" sort="Caron, C" uniqKey="Caron C" first="C." last="Caron">C. Caron</name><affiliation><mods:affiliation>Laboratoire d’hématologie, Hôpital Régional et Universitaire, Lille, France</mods:affiliation></affiliation></author><author><name sortKey="Burkhardt, T" sort="Burkhardt, T" uniqKey="Burkhardt T" first="T." last="Burkhardt">T. Burkhardt</name><affiliation><mods:affiliation>Red Cross Blood Transfusion Center Saxony, Plauen, Germany</mods:affiliation></affiliation></author><author><name sortKey="Goudemand, J" sort="Goudemand, J" uniqKey="Goudemand J" first="J." last="Goudemand">J. Goudemand</name><affiliation><mods:affiliation>Laboratoire d’hématologie, Hôpital Régional et Universitaire, Lille, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Vox Sanguinis</title><title level="j" type="alt">VOX SANGUINIS</title><idno type="ISSN">0042-9007</idno><idno type="eISSN">1423-0410</idno><imprint><biblScope unit="vol">87</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="27">27</biblScope><biblScope unit="page" to="33">33</biblScope><biblScope unit="page-count">7</biblScope><publisher>Blackwell Science Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2004-07">2004-07</date></imprint><idno type="ISSN">0042-9007</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-9007</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Apheresis</term><term>Apheresis plasma</term><term>Apheresis plasmas</term><term>Apheresis procedures</term><term>Assay</term><term>Blackwell publishing</term><term>Blood group</term><term>Burnouf</term><term>Collagen binding activity</term><term>Cryoprecipitate</term><term>Donation</term><term>Factor viii</term><term>Functional activity</term><term>Greater number</term><term>Largest multimers</term><term>Lter core</term><term>Mers</term><term>Multimeric structure</term><term>Multimers</term><term>Normal plasma</term><term>Normal plasma pools</term><term>Npps</term><term>Plasma</term><term>Plasma donations</term><term>Plasma units</term><term>Platelet</term><term>Reference plasma</term><term>Respective pools</term><term>Sanguinis</term><term>Secondary haemostasis</term><term>Source plasma</term><term>Thromb</term><term>Thromb haemost</term><term>Transfusion</term><term>Viii</term><term>Willebrand</term><term>Willebrand disease</term><term>Willebrand factor</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Background and Objectives Von Willebrand Factor (VWF) is a complex high‐molecular‐weight (HMW) plasma glycoprotein playing a critical role in primary and secondary haemostasis. Owing to its multimeric structure and sensitivity to proteolysis, VWF can be used as a marker of the impact of collection procedures on the characteristics of plasma for transfusion and for fractionation. We studied VWF content, functional activity and HMW multimers in plasmas collected by five different automated apheresis collection procedures. Materials and Methods Five series of 30 plasma units were obtained from volunteer donors at two collection sites using Haemonetics PCS2 machines with Revision (Rev) F, Rev G, high‐separation core (HSC), or filter core (FC) procedures, or Baxter‐Fenwall Autopheresis‐C (Auto‐C). VWF antigen (VWF:Ag), ristocetin cofactor (VWF:RCo) activity and HMW multimers were first determined in 10 randomly selected plasma donations collected with Rev G, HSC, FC and Auto‐C procedures. Then, the same analyses and the collagen binding (VWF:CB) activity were determined in the pools of 30 donations from each of the five procedures and compared with two normal plasma pools (NPP1 and NPP2). A reference plasma (RP) was used to calibrate each assay. Results There were a greater number of group O individuals in the Rev F, Rev G and FC donors than in the HSC and Auto‐C donors. The mean VWF:Ag level was > 100 IU/dl, VWF:RCo activity was > 90 U/dl, the VWF:RCo/Ag ratio was close to 1, and the percentage of 11–15 mers was above 100% of RP in the 10 individual plasma units from Rev G, HSC, FC, and Auto‐C and in their respective pools. The mean percentage of multimers > 15 mers, relative to RP, was significantly less in Rev G plasmas (48 ± 17%; range 32–91%), compared with Auto‐C, HSC and FC plasmas (P = 0·0211; 0·0257; and 0·0376, respectively). The VWF:CB activity of the 30‐donation pools was 61 and 60 U/dl in Auto C and HSC, 50 U/dl in Rev F and FC, and 43 U/dl in the Rev G pool. The VWF:CB/Ag ratio was 0·54 (Auto‐C), 0·49 (HSC), 0·46 (Rev F), 0·45 (FC) and 0·37 (Rev G), compared with 0·81and 0·92 in NPPs. The percentage of VWF multimers of 11–15 mers in apheresis plasma and NPP was normal. VWF multimers > 15 mers ranged from 38 to 64% of that of RP plasma, and was 111 and 112% in NPPs. Conclusions The VWF:Ag, VWF:RCo activity and 11–15 mer VWF multimers were well preserved in all plasma units from each of the five apheresis procedures. The VWF:CB activity and the percentage of multimers > 15 mers in apheresis plasma was less than in normal plasma pools and differed slightly among procedures.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>willebrand</json:string><json:string>multimers</json:string><json:string>apheresis</json:string><json:string>willebrand factor</json:string><json:string>mers</json:string><json:string>willebrand disease</json:string><json:string>platelet</json:string><json:string>viii</json:string><json:string>cryoprecipitate</json:string><json:string>npps</json:string><json:string>burnouf</json:string><json:string>sanguinis</json:string><json:string>thromb</json:string><json:string>transfusion</json:string><json:string>apheresis plasma</json:string><json:string>blackwell publishing</json:string><json:string>assay</json:string><json:string>functional activity</json:string><json:string>blood group</json:string><json:string>factor viii</json:string><json:string>normal plasma</json:string><json:string>apheresis procedures</json:string><json:string>lter core</json:string><json:string>thromb haemost</json:string><json:string>reference plasma</json:string><json:string>greater number</json:string><json:string>respective pools</json:string><json:string>plasma units</json:string><json:string>plasma</json:string><json:string>donation</json:string><json:string>secondary haemostasis</json:string><json:string>normal plasma pools</json:string><json:string>plasma donations</json:string><json:string>apheresis plasmas</json:string><json:string>largest multimers</json:string><json:string>collagen binding activity</json:string><json:string>source plasma</json:string><json:string>multimeric structure</json:string></teeft></keywords><author><json:item><name>T. Burnouf</name><affiliations><json:string>Human Plasma Product Services, Lille, France</json:string><json:string>E-mail: tburnou@attglobal.net</json:string></affiliations></json:item><json:item><name>C. Caron</name><affiliations><json:string>Laboratoire d’hématologie, Hôpital Régional et Universitaire, Lille, France</json:string></affiliations></json:item><json:item><name>T. Burkhardt</name><affiliations><json:string>Red Cross Blood Transfusion Center Saxony, Plauen, Germany</json:string></affiliations></json:item><json:item><name>J. Goudemand</name><affiliations><json:string>Laboratoire d’hématologie, Hôpital Régional et Universitaire, Lille, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>apheresis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>collagen binding</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>multimers</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>plasma</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>ristocetin cofactor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>von Willebrand factor</value></json:item></subject><articleId><json:string>VOX535</json:string></articleId><arkIstex>ark:/67375/WNG-XR0H5S0N-M</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Background and Objectives Von Willebrand Factor (VWF) is a complex high‐molecular‐weight (HMW) plasma glycoprotein playing a critical role in primary and secondary haemostasis. Owing to its multimeric structure and sensitivity to proteolysis, VWF can be used as a marker of the impact of collection procedures on the characteristics of plasma for transfusion and for fractionation. We studied VWF content, functional activity and HMW multimers in plasmas collected by five different automated apheresis collection procedures. Materials and Methods Five series of 30 plasma units were obtained from volunteer donors at two collection sites using Haemonetics PCS2 machines with Revision (Rev) F, Rev G, high‐separation core (HSC), or filter core (FC) procedures, or Baxter‐Fenwall Autopheresis‐C (Auto‐C). VWF antigen (VWF:Ag), ristocetin cofactor (VWF:RCo) activity and HMW multimers were first determined in 10 randomly selected plasma donations collected with Rev G, HSC, FC and Auto‐C procedures. Then, the same analyses and the collagen binding (VWF:CB) activity were determined in the pools of 30 donations from each of the five procedures and compared with two normal plasma pools (NPP1 and NPP2). A reference plasma (RP) was used to calibrate each assay. Results There were a greater number of group O individuals in the Rev F, Rev G and FC donors than in the HSC and Auto‐C donors. The mean VWF:Ag level was > 100 IU/dl, VWF:RCo activity was > 90 U/dl, the VWF:RCo/Ag ratio was close to 1, and the percentage of 11–15 mers was above 100% of RP in the 10 individual plasma units from Rev G, HSC, FC, and Auto‐C and in their respective pools. The mean percentage of multimers > 15 mers, relative to RP, was significantly less in Rev G plasmas (48 ± 17%; range 32–91%), compared with Auto‐C, HSC and FC plasmas (P = 0·0211; 0·0257; and 0·0376, respectively). The VWF:CB activity of the 30‐donation pools was 61 and 60 U/dl in Auto C and HSC, 50 U/dl in Rev F and FC, and 43 U/dl in the Rev G pool. The VWF:CB/Ag ratio was 0·54 (Auto‐C), 0·49 (HSC), 0·46 (Rev F), 0·45 (FC) and 0·37 (Rev G), compared with 0·81and 0·92 in NPPs. The percentage of VWF multimers of 11–15 mers in apheresis plasma and NPP was normal. VWF multimers > 15 mers ranged from 38 to 64% of that of RP plasma, and was 111 and 112% in NPPs. Conclusions The VWF:Ag, VWF:RCo activity and 11–15 mer VWF multimers were well preserved in all plasma units from each of the five apheresis procedures. The VWF:CB activity and the percentage of multimers > 15 mers in apheresis plasma was less than in normal plasma pools and differed slightly among procedures.</abstract><qualityIndicators><score>9.089</score><pdfWordCount>4089</pdfWordCount><pdfCharCount>25294</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>595 x 782 pts</pdfPageSize><pdfWordsPerPage>584</pdfWordsPerPage><pdfText>true</pdfText><refBibsNative>true</refBibsNative><abstractWordCount>429</abstractWordCount><abstractCharCount>2630</abstractCharCount><keywordCount>6</keywordCount></qualityIndicators><title>Content and functional activity of von Willebrand factor in apheresis plasma</title><pmid><json:string>15260819</json:string></pmid><genre><json:string>article</json:string></genre><host><title>Vox Sanguinis</title><language><json:string>unknown</json:string></language><doi><json:string>10.1111/(ISSN)1423-0410</json:string></doi><issn><json:string>0042-9007</json:string></issn><eissn><json:string>1423-0410</json:string></eissn><publisherId><json:string>VOX</json:string></publisherId><volume>87</volume><issue>1</issue><pages><first>27</first><last>33</last><total>7</total></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>2004</json:string></date><geogName></geogName><orgName><json:string>Baxter Corporation</json:string><json:string>France Laboratoire</json:string><json:string>Red Cross Blood Transfusion Center Saxony, Plauen, Germany</json:string><json:string>Haemonetics Corporation</json:string><json:string>Blackwell Publishing Ltd</json:string><json:string>France, Lille</json:string><json:string>UK Blackwell T</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Sylvie Hermoire</json:string><json:string>Dr Peter</json:string><json:string>Thierry Burnouf</json:string><json:string>J. Goudemand</json:string></persName><placeName><json:string>Saint Jacques</json:string><json:string>Paris</json:string><json:string>Germany</json:string><json:string>Nancy</json:string><json:string>Braintree</json:string><json:string>Plauen</json:string><json:string>Denmark</json:string><json:string>MA</json:string><json:string>France</json:string><json:string>Lille</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[4]</json:string><json:string>[18]</json:string><json:string>[6]</json:string><json:string>[33]</json:string><json:string>[31,32]</json:string><json:string>[8]</json:string><json:string>[39]</json:string><json:string>[14,15]</json:string><json:string>Burnouf et al. 2004</json:string><json:string>[1]</json:string><json:string>T. Burnouf et al.</json:string><json:string>[21]</json:string><json:string>[8,9]</json:string><json:string>[38]</json:string><json:string>[3]</json:string><json:string>[20]</json:string><json:string>[5]</json:string><json:string>[26]</json:string><json:string>[16,18]</json:string><json:string>[23,24]</json:string><json:string>[6,7]</json:string><json:string>[41]</json:string><json:string>[19,20]</json:string><json:string>[40]</json:string><json:string>[2]</json:string><json:string>[29,30]</json:string><json:string>[19]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/WNG-XR0H5S0N-M</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - hematology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - clinical medicine</json:string><json:string>3 - cardiovascular system & hematology</json:string></scienceMetrix><scopus><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - Hematology</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - General Medicine</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences medicales</json:string></inist></categories><publicationDate>2004</publicationDate><copyrightDate>2004</copyrightDate><doi><json:string>10.1111/j.1423-0410.2004.00535.x</json:string></doi><id>D32E13F98B080996EE2C1EC4A23A9B3BA6290E7D</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-XR0H5S0N-M/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-XR0H5S0N-M/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/WNG-XR0H5S0N-M/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">Content and functional activity of von Willebrand factor in apheresis plasma</title><title level="a" type="short">Von Willebrand factor in apheresis plasma</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Blackwell Science Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2004-07"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main">Content and functional activity of von Willebrand factor in apheresis plasma</title><title level="a" type="short">Von Willebrand factor in apheresis plasma</title><author xml:id="author-0000" role="corresp"><persName><forename type="first">T.</forename><surname>Burnouf</surname></persName><affiliation><orgName type="laboratory">Human Plasma Product Services</orgName><address><addrLine>Lille</addrLine><addrLine>France</addrLine><country key="FR" xml:lang="en">FRANCE</country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">C.</forename><surname>Caron</surname></persName><affiliation><orgName type="laboratory">Laboratoire d’hématologie</orgName><orgName type="institution">Hôpital Régional et Universitaire</orgName><address><addrLine>Lille</addrLine><addrLine>France</addrLine><country key="FR" xml:lang="en">FRANCE</country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">T.</forename><surname>Burkhardt</surname></persName><affiliation><orgName type="institution">Red Cross Blood Transfusion Center Saxony</orgName><address><addrLine>Plauen</addrLine><addrLine>Germany</addrLine><country key="DE" xml:lang="en">GERMANY</country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">J.</forename><surname>Goudemand</surname></persName><affiliation><orgName type="laboratory">Laboratoire d’hématologie</orgName><orgName type="institution">Hôpital Régional et Universitaire</orgName><address><addrLine>Lille</addrLine><addrLine>France</addrLine><country key="FR" xml:lang="en">FRANCE</country></address></affiliation></author><idno type="istex">D32E13F98B080996EE2C1EC4A23A9B3BA6290E7D</idno><idno type="ark">ark:/67375/WNG-XR0H5S0N-M</idno><idno type="DOI">10.1111/j.1423-0410.2004.00535.x</idno><idno type="unit">VOX535</idno><idno type="toTypesetVersion">file:VOX.VOX535.pdf</idno></analytic><monogr><title level="j" type="main">Vox Sanguinis</title><title level="j" type="alt">VOX SANGUINIS</title><idno type="pISSN">0042-9007</idno><idno type="eISSN">1423-0410</idno><idno type="book-DOI">10.1111/(ISSN)1423-0410</idno><idno type="book-part-DOI">10.1111/vox.2004.87.issue-1</idno><idno type="product">VOX</idno><idno type="publisherDivision">ST</idno><imprint><biblScope unit="vol">87</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="27">27</biblScope><biblScope unit="page" to="33">33</biblScope><biblScope unit="page-count">7</biblScope><publisher>Blackwell Science Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2004-07"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><encodingDesc><schemaRef type="ODD" url="https://xml-schema.delivery.istex.fr/tei-istex.odd"></schemaRef><appInfo><application ident="pub2tei" version="1.0.10" when="2019-12-20"><label>pub2TEI-ISTEX</label><desc>A set of style sheets for converting XML documents encoded in various scientific publisher formats into a common TEI format.
<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract xml:lang="en" style="main"><p><hi rend="bold">Background and Objectives </hi> Von Willebrand Factor (VWF) is a complex high‐molecular‐weight (HMW) plasma glycoprotein playing a critical role in primary and secondary haemostasis. Owing to its multimeric structure and sensitivity to proteolysis, VWF can be used as a marker of the impact of collection procedures on the characteristics of plasma for transfusion and for fractionation. We studied VWF content, functional activity and HMW multimers in plasmas collected by five different automated apheresis collection procedures.</p><p><hi rend="bold">Materials and Methods </hi> Five series of 30 plasma units were obtained from volunteer donors at two collection sites using Haemonetics PCS2 machines with Revision (Rev) F, Rev G, high‐separation core (HSC), or filter core (FC) procedures, or Baxter‐Fenwall Autopheresis‐C (Auto‐C). VWF antigen (VWF:Ag), ristocetin cofactor (VWF:RCo) activity and HMW multimers were first determined in 10 randomly selected plasma donations collected with Rev G, HSC, FC and Auto‐C procedures. Then, the same analyses and the collagen binding (VWF:CB) activity were determined in the pools of 30 donations from each of the five procedures and compared with two normal plasma pools (NPP1 and NPP2). A reference plasma (RP) was used to calibrate each assay.</p><p><hi rend="bold">Results </hi> There were a greater number of group O individuals in the Rev F, Rev G and FC donors than in the HSC and Auto‐C donors. The mean VWF:Ag level was > 100 IU/dl, VWF:RCo activity was > 90 U/dl, the VWF:RCo/Ag ratio was close to 1, and the percentage of 11–15 mers was above 100% of RP in the 10 individual plasma units from Rev G, HSC, FC, and Auto‐C and in their respective pools. The mean percentage of multimers > 15 mers, relative to RP, was significantly less in Rev G plasmas (48 ± 17%; range 32–91%), compared with Auto‐C, HSC and FC plasmas (<hi rend="italic">P</hi> = 0·0211; 0·0257; and 0·0376, respectively). The VWF:CB activity of the 30‐donation pools was 61 and 60 U/dl in Auto C and HSC, 50 U/dl in Rev F and FC, and 43 U/dl in the Rev G pool. The VWF:CB/Ag ratio was 0·54 (Auto‐C), 0·49 (HSC), 0·46 (Rev F), 0·45 (FC) and 0·37 (Rev G), compared with 0·81and 0·92 in NPPs. The percentage of VWF multimers of 11–15 mers in apheresis plasma and NPP was normal. VWF multimers > 15 mers ranged from 38 to 64% of that of RP plasma, and was 111 and 112% in NPPs.</p><p><hi rend="bold">Conclusions </hi> The VWF:Ag, VWF:RCo activity and 11–15 mer VWF multimers were well preserved in all plasma units from each of the five apheresis procedures. The VWF:CB activity and the percentage of multimers > 15 mers in apheresis plasma was less than in normal plasma pools and differed slightly among procedures.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">apheresis</term><term xml:id="k2">collagen binding</term><term xml:id="k3">multimers</term><term xml:id="k4">plasma</term><term xml:id="k5">ristocetin cofactor</term><term xml:id="k6">von Willebrand factor</term></keywords><keywords rend="tocHeading1"><term>Blood Component Collection and Production</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-XR0H5S0N-M/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Science Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1423-0410</doi><issn type="print">0042-9007</issn><issn type="electronic">1423-0410</issn><idGroup><id type="product" value="VOX"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="VOX SANGUINIS">Vox Sanguinis</title></titleGroup></publicationMeta><publicationMeta level="part" position="07001"><doi origin="wiley">10.1111/vox.2004.87.issue-1</doi><numberingGroup><numbering type="journalVolume" number="87">87</numbering><numbering type="journalIssue" number="1">1</numbering></numberingGroup><coverDate startDate="2004-07">July 2004</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="4" status="forIssue"><doi origin="wiley">10.1111/j.1423-0410.2004.00535.x</doi><idGroup><id type="unit" value="VOX535"></id></idGroup><countGroup><count type="pageTotal" number="7"></count></countGroup><titleGroup><title type="tocHeading1">Blood Component Collection and Production</title></titleGroup><eventGroup><event type="firstOnline" date="2004-07-16"></event><event type="publishedOnlineFinalForm" date="2004-07-16"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.5 mode:FullText source:FullText result:FullText" date="2010-04-06"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-10"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-11-04"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="27">27</numbering><numbering type="pageLast" number="33">33</numbering></numberingGroup><correspondenceTo><i>Correspondence</i>: Thierry Burnouf, HPPS, 18, rue Saint Jacques, 59000 Lille, France
E‐mail: <email>tburnou@attglobal.net</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:VOX.VOX535.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received: 11 March 2004, revised 13 May 2004, accepted 16 May 2004</unparsedEditorialHistory><countGroup><count type="figureTotal" number="1"></count><count type="tableTotal" number="2"></count><count type="formulaTotal" number="0"></count><count type="referenceTotal" number="41"></count><count type="wordTotal" number="2927"></count></countGroup><titleGroup><title type="main">Content and functional activity of von Willebrand factor in apheresis plasma</title><title type="shortAuthors">T. Burnouf <i>et al.</i></title><title type="short">Von Willebrand factor in apheresis plasma</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1" corresponding="yes"><personName><givenNames>T.</givenNames><familyName>Burnouf</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a2"><personName><givenNames>C.</givenNames><familyName>Caron</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a3"><personName><givenNames>T.</givenNames><familyName>Burkhardt</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a2"><personName><givenNames>J.</givenNames><familyName>Goudemand</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="FR"><unparsedAffiliation>Human Plasma Product Services, Lille, France</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="FR"><unparsedAffiliation>Laboratoire d’hématologie, Hôpital Régional et Universitaire, Lille, France</unparsedAffiliation></affiliation><affiliation xml:id="a3" countryCode="DE"><unparsedAffiliation>Red Cross Blood Transfusion Center Saxony, Plauen, Germany</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">apheresis</keyword><keyword xml:id="k2">collagen binding</keyword><keyword xml:id="k3">multimers</keyword><keyword xml:id="k4">plasma</keyword><keyword xml:id="k5">ristocetin cofactor</keyword><keyword xml:id="k6">von Willebrand factor</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p><b>Background and Objectives </b> Von Willebrand Factor (VWF) is a complex high‐molecular‐weight (HMW) plasma glycoprotein playing a critical role in primary and secondary haemostasis. Owing to its multimeric structure and sensitivity to proteolysis, VWF can be used as a marker of the impact of collection procedures on the characteristics of plasma for transfusion and for fractionation. We studied VWF content, functional activity and HMW multimers in plasmas collected by five different automated apheresis collection procedures.</p><p><b>Materials and Methods </b> Five series of 30 plasma units were obtained from volunteer donors at two collection sites using Haemonetics PCS2 machines with Revision (Rev) F, Rev G, high‐separation core (HSC), or filter core (FC) procedures, or Baxter‐Fenwall Autopheresis‐C (Auto‐C). VWF antigen (VWF:Ag), ristocetin cofactor (VWF:RCo) activity and HMW multimers were first determined in 10 randomly selected plasma donations collected with Rev G, HSC, FC and Auto‐C procedures. Then, the same analyses and the collagen binding (VWF:CB) activity were determined in the pools of 30 donations from each of the five procedures and compared with two normal plasma pools (NPP1 and NPP2). A reference plasma (RP) was used to calibrate each assay.</p><p><b>Results </b> There were a greater number of group O individuals in the Rev F, Rev G and FC donors than in the HSC and Auto‐C donors. The mean VWF:Ag level was > 100 IU/dl, VWF:RCo activity was > 90 U/dl, the VWF:RCo/Ag ratio was close to 1, and the percentage of 11–15 mers was above 100% of RP in the 10 individual plasma units from Rev G, HSC, FC, and Auto‐C and in their respective pools. The mean percentage of multimers > 15 mers, relative to RP, was significantly less in Rev G plasmas (48 ± 17%; range 32–91%), compared with Auto‐C, HSC and FC plasmas (<i>P</i> = 0·0211; 0·0257; and 0·0376, respectively). The VWF:CB activity of the 30‐donation pools was 61 and 60 U/dl in Auto C and HSC, 50 U/dl in Rev F and FC, and 43 U/dl in the Rev G pool. The VWF:CB/Ag ratio was 0·54 (Auto‐C), 0·49 (HSC), 0·46 (Rev F), 0·45 (FC) and 0·37 (Rev G), compared with 0·81and 0·92 in NPPs. The percentage of VWF multimers of 11–15 mers in apheresis plasma and NPP was normal. VWF multimers > 15 mers ranged from 38 to 64% of that of RP plasma, and was 111 and 112% in NPPs.</p><p><b>Conclusions </b> The VWF:Ag, VWF:RCo activity and 11–15 mer VWF multimers were well preserved in all plasma units from each of the five apheresis procedures. The VWF:CB activity and the percentage of multimers > 15 mers in apheresis plasma was less than in normal plasma pools and differed slightly among procedures.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Content and functional activity of von Willebrand factor in apheresis plasma</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Von Willebrand factor in apheresis plasma</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Content and functional activity of von Willebrand factor in apheresis plasma</title></titleInfo><name type="personal"><namePart type="given">T.</namePart><namePart type="family">Burnouf</namePart><affiliation>Human Plasma Product Services, Lille, France</affiliation><affiliation>E-mail: tburnou@attglobal.net</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C.</namePart><namePart type="family">Caron</namePart><affiliation>Laboratoire d’hématologie, Hôpital Régional et Universitaire, Lille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">T.</namePart><namePart type="family">Burkhardt</namePart><affiliation>Red Cross Blood Transfusion Center Saxony, Plauen, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Goudemand</namePart><affiliation>Laboratoire d’hématologie, Hôpital Régional et Universitaire, Lille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Science Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">2004-07</dateIssued><edition>Received: 11 March 2004, revised 13 May 2004, accepted 16 May 2004</edition><copyrightDate encoding="w3cdtf">2004</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">1</extent><extent unit="tables">2</extent><extent unit="formulas">0</extent><extent unit="references">41</extent><extent unit="words">2927</extent></physicalDescription><abstract lang="en">Background and Objectives Von Willebrand Factor (VWF) is a complex high‐molecular‐weight (HMW) plasma glycoprotein playing a critical role in primary and secondary haemostasis. Owing to its multimeric structure and sensitivity to proteolysis, VWF can be used as a marker of the impact of collection procedures on the characteristics of plasma for transfusion and for fractionation. We studied VWF content, functional activity and HMW multimers in plasmas collected by five different automated apheresis collection procedures. Materials and Methods Five series of 30 plasma units were obtained from volunteer donors at two collection sites using Haemonetics PCS2 machines with Revision (Rev) F, Rev G, high‐separation core (HSC), or filter core (FC) procedures, or Baxter‐Fenwall Autopheresis‐C (Auto‐C). VWF antigen (VWF:Ag), ristocetin cofactor (VWF:RCo) activity and HMW multimers were first determined in 10 randomly selected plasma donations collected with Rev G, HSC, FC and Auto‐C procedures. Then, the same analyses and the collagen binding (VWF:CB) activity were determined in the pools of 30 donations from each of the five procedures and compared with two normal plasma pools (NPP1 and NPP2). A reference plasma (RP) was used to calibrate each assay. Results There were a greater number of group O individuals in the Rev F, Rev G and FC donors than in the HSC and Auto‐C donors. The mean VWF:Ag level was > 100 IU/dl, VWF:RCo activity was > 90 U/dl, the VWF:RCo/Ag ratio was close to 1, and the percentage of 11–15 mers was above 100% of RP in the 10 individual plasma units from Rev G, HSC, FC, and Auto‐C and in their respective pools. The mean percentage of multimers > 15 mers, relative to RP, was significantly less in Rev G plasmas (48 ± 17%; range 32–91%), compared with Auto‐C, HSC and FC plasmas (P = 0·0211; 0·0257; and 0·0376, respectively). The VWF:CB activity of the 30‐donation pools was 61 and 60 U/dl in Auto C and HSC, 50 U/dl in Rev F and FC, and 43 U/dl in the Rev G pool. The VWF:CB/Ag ratio was 0·54 (Auto‐C), 0·49 (HSC), 0·46 (Rev F), 0·45 (FC) and 0·37 (Rev G), compared with 0·81and 0·92 in NPPs. The percentage of VWF multimers of 11–15 mers in apheresis plasma and NPP was normal. VWF multimers > 15 mers ranged from 38 to 64% of that of RP plasma, and was 111 and 112% in NPPs. Conclusions The VWF:Ag, VWF:RCo activity and 11–15 mer VWF multimers were well preserved in all plasma units from each of the five apheresis procedures. The VWF:CB activity and the percentage of multimers > 15 mers in apheresis plasma was less than in normal plasma pools and differed slightly among procedures.</abstract><subject lang="en"><genre>keywords</genre><topic>apheresis</topic><topic>collagen binding</topic><topic>multimers</topic><topic>plasma</topic><topic>ristocetin cofactor</topic><topic>von Willebrand factor</topic></subject><relatedItem type="host"><titleInfo><title>Vox Sanguinis</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><identifier type="ISSN">0042-9007</identifier><identifier type="eISSN">1423-0410</identifier><identifier type="DOI">10.1111/(ISSN)1423-0410</identifier><identifier type="PublisherID">VOX</identifier><part><date>2004</date><detail type="volume"><caption>vol.</caption><number>87</number></detail><detail type="issue"><caption>no.</caption><number>1</number></detail><extent unit="pages"><start>27</start><end>33</end><total>7</total></extent></part></relatedItem><relatedItem type="references" displayLabel="cit1"><titleInfo><title>Von Willebrand factor: molecular size and functional activity</title></titleInfo><name type="personal"><namePart type="given">M</namePart><namePart type="family">Furlan</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Furlan M: Von Willebrand factor: molecular size and functional activity. 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Favourable effects of heating on the von Willebrand factor. Vox Sang 1987; 52: 265–271</note><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>52</number></detail><extent unit="pages"><start>265</start><end>271</end></extent></part><relatedItem type="host"><titleInfo><title>Vox Sang</title></titleInfo><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>52</number></detail><extent unit="pages"><start>265</start><end>271</end></extent></part></relatedItem></relatedItem><identifier type="istex">D32E13F98B080996EE2C1EC4A23A9B3BA6290E7D</identifier><identifier type="ark">ark:/67375/WNG-XR0H5S0N-M</identifier><identifier type="DOI">10.1111/j.1423-0410.2004.00535.x</identifier><identifier type="ArticleID">VOX535</identifier><accessCondition type="use and reproduction" contentType="copyright">© Wiley. 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