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Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis
Recombinant Factor VIII (rFVIII) is involved in the cascade of biochemical reactions leading to blood coagulation and is used for the treatment of haemophilia A. Plasma‐derived FVIII (pdFVIII) has been reported to be post‐translationally modified by sulfation of tyrosine residues at positions 346, 1...
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Published in: | Rapid communications in mass spectrometry 1999-01, Vol.13 (11), p.1016-1023 |
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creator | Severs, Joanne C. Carnine, Mechelle Eguizabal, Hugo Mock, Kuldip K. |
description | Recombinant Factor VIII (rFVIII) is involved in the cascade of biochemical reactions leading to blood coagulation and is used for the treatment of haemophilia A. Plasma‐derived FVIII (pdFVIII) has been reported to be post‐translationally modified by sulfation of tyrosine residues at positions 346, 1664, 1680, 718, 719 and 723.1 This report describes the quantitation of tyrosine sulfate residues in BHK‐derived, human rFVIII by amino acid composition analysis and the identification of their positions in the polypeptide sequence using a combination of liquid chromatography and electrospray ionization mass spectrometry in the analysis of proteolytic digests of the protein. Copyright © 1999 John Wiley & Sons, Ltd. |
doi_str_mv | 10.1002/(SICI)1097-0231(19990615)13:11<1016::AID-RCM599>3.0.CO;2-5 |
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Plasma‐derived FVIII (pdFVIII) has been reported to be post‐translationally modified by sulfation of tyrosine residues at positions 346, 1664, 1680, 718, 719 and 723.1 This report describes the quantitation of tyrosine sulfate residues in BHK‐derived, human rFVIII by amino acid composition analysis and the identification of their positions in the polypeptide sequence using a combination of liquid chromatography and electrospray ionization mass spectrometry in the analysis of proteolytic digests of the protein. 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Mass Spectrom</addtitle><description>Recombinant Factor VIII (rFVIII) is involved in the cascade of biochemical reactions leading to blood coagulation and is used for the treatment of haemophilia A. Plasma‐derived FVIII (pdFVIII) has been reported to be post‐translationally modified by sulfation of tyrosine residues at positions 346, 1664, 1680, 718, 719 and 723.1 This report describes the quantitation of tyrosine sulfate residues in BHK‐derived, human rFVIII by amino acid composition analysis and the identification of their positions in the polypeptide sequence using a combination of liquid chromatography and electrospray ionization mass spectrometry in the analysis of proteolytic digests of the protein. Copyright © 1999 John Wiley & Sons, Ltd.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Factor VIII - analysis</subject><subject>Hydrolysis</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - analysis</subject><subject>Peptide Mapping</subject><subject>Recombinant Proteins - analysis</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Thrombin - chemistry</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - analysis</subject><issn>0951-4198</issn><issn>1097-0231</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqNkV2L1DAUhoso7rj6FyRXsnvRMadp2skowtrVsbA64CcMwiFNUyfar006rPWf-e_M2NlF0AsvQsnp2-dN8wTBc6BzoDR6fPIuz_JToCINacTgBIQQNAF-CmwJ8BQoJMvlWX4evs1ecyGesTmdZ-snUchvBbObz24HMyo4hDGIxVFwz7mvlALwiN4NjoCyZCHSdBb8zLbSSjVoa37IwXQt6SoyjLZzptXE7epKDppY7Uy5046Ylsh2MFvddP3W1Eb5V6prCtP6Mak8qLPkY57npBhJbS53piRqa7tGDt0XK_vtSHSt1eD5vZUj8YXXvYNsS92QRjpHXP870-jBjr6wJLIxbUek8jjZynp0xt0P7lSydvrB4XkcfHj54n32KrxYr_Ls7CJUMTARlmlccK4pq0BECTApoFokWi38DSRpVaVloisRy0hxqXhUFSLiPknjWCQp0IIdB48mbm-7S38HAzbGKV3XstXdzmEiFpFHJT64mYLK_52zusLemkbaEYHiXiziXizuDeHeEF6LRWAIfuvFInqxOIlFhhSzNUbIPfzh4RS7otHlH-jJpA98ngJXptbjX9X_0fzP4sPE48MJb9ygv9_gpf2GScpSjp_erPyCeJVuMtywX4dX1DY</recordid><startdate>19990101</startdate><enddate>19990101</enddate><creator>Severs, Joanne C.</creator><creator>Carnine, Mechelle</creator><creator>Eguizabal, Hugo</creator><creator>Mock, Kuldip K.</creator><general>John Wiley & Sons, Ltd</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19990101</creationdate><title>Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis</title><author>Severs, Joanne C. ; Carnine, Mechelle ; Eguizabal, Hugo ; Mock, Kuldip K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4139-d74b55e03f192613a91f86ec836867ff7d6ef94a2c5ac52fb92519204496710b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Factor VIII - analysis</topic><topic>Hydrolysis</topic><topic>Mass Spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - analysis</topic><topic>Peptide Mapping</topic><topic>Recombinant Proteins - analysis</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Thrombin - chemistry</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Severs, Joanne C.</creatorcontrib><creatorcontrib>Carnine, Mechelle</creatorcontrib><creatorcontrib>Eguizabal, Hugo</creatorcontrib><creatorcontrib>Mock, Kuldip K.</creatorcontrib><collection>Istex</collection><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>Rapid communications in mass spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Severs, Joanne C.</au><au>Carnine, Mechelle</au><au>Eguizabal, Hugo</au><au>Mock, Kuldip K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis</atitle><jtitle>Rapid communications in mass spectrometry</jtitle><addtitle>Rapid Commun. 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Copyright © 1999 John Wiley & Sons, Ltd.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>10368977</pmid><doi>10.1002/(SICI)1097-0231(19990615)13:11<1016::AID-RCM599>3.0.CO;2-5</doi><tpages>8</tpages></addata></record> |
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source | Wiley-Blackwell Read & Publish Collection |
subjects | Amino Acid Sequence Amino Acids - analysis Chromatography, High Pressure Liquid Factor VIII - analysis Hydrolysis Mass Spectrometry Molecular Sequence Data Peptide Fragments - analysis Peptide Mapping Recombinant Proteins - analysis Spectrophotometry, Ultraviolet Thrombin - chemistry Tyrosine - analogs & derivatives Tyrosine - analysis |
title | Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis |
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