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Pig tissue factor pathway inhibitor alpha fusion immunoglobulin inhibits pig tissue factor activity in human plasma moderately more efficiently than the human counterpart

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dc.contributor.authorChoi, Chang-Yong-
dc.contributor.authorKim, Yeon-Hui-
dc.contributor.authorBae, Joonbeom-
dc.contributor.authorLee, Suk Jun-
dc.contributor.authorKim, Hyun Kyung-
dc.contributor.authorPark, Chung-Gyu-
dc.contributor.authorChun, Taehoon-
dc.date.accessioned2021-09-02T23:53:21Z-
dc.date.available2021-09-02T23:53:21Z-
dc.date.created2021-06-19-
dc.date.issued2017-11-
dc.identifier.issn0141-5492-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/81789-
dc.description.abstractTo determine the efficacy of soluble pig tissue factor pathway inhibitor fusion immunoglobulin (TFPI-Ig) in blocking pig to human xenogeneic blood coagulation. To generate pig TFPI-Ig or human TFPI-Ig, expression vector containing cDNA encoding pig TFPI alpha or human TFPI alpha combined with human constant Ig heavy chain region was cloned and introduced into CHO cells. After purification of pig TFPI-Ig and human TFPI-Ig, the inhibition of each recombinant protein on pig tissue factor (TF)-mediated blood coagulation was examined in human plasma. Compared to human TFPI-Ig, pig TFPI-Ig inhibited pig TF activity and thrombin generation in human plasma more efficiently at certain concentrations. Pig TFPI-Ig will be be useful as a therapeutic protein to treat pig to human xenogeneic blood coagulation.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherSPRINGER-
dc.subjectCOAGULATION INHIBITOR-
dc.subjectFACTOR-XA-
dc.subjectDEGRADATION-
dc.subjectEXPRESSION-
dc.subjectDOMAINS-
dc.subjectISLETS-
dc.titlePig tissue factor pathway inhibitor alpha fusion immunoglobulin inhibits pig tissue factor activity in human plasma moderately more efficiently than the human counterpart-
dc.typeArticle-
dc.contributor.affiliatedAuthorChoi, Chang-Yong-
dc.contributor.affiliatedAuthorChun, Taehoon-
dc.identifier.doi10.1007/s10529-017-2405-3-
dc.identifier.scopusid2-s2.0-85026916923-
dc.identifier.wosid000412733200004-
dc.identifier.bibliographicCitationBIOTECHNOLOGY LETTERS, v.39, no.11, pp.1631 - 1638-
dc.relation.isPartOfBIOTECHNOLOGY LETTERS-
dc.citation.titleBIOTECHNOLOGY LETTERS-
dc.citation.volume39-
dc.citation.number11-
dc.citation.startPage1631-
dc.citation.endPage1638-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiotechnology & Applied Microbiology-
dc.relation.journalWebOfScienceCategoryBiotechnology & Applied Microbiology-
dc.subject.keywordPlusCOAGULATION INHIBITOR-
dc.subject.keywordPlusFACTOR-XA-
dc.subject.keywordPlusDEGRADATION-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusDOMAINS-
dc.subject.keywordPlusISLETS-
dc.subject.keywordAuthorBlood coagulation-
dc.subject.keywordAuthorRecombinant protein-
dc.subject.keywordAuthorTissue factor-
dc.subject.keywordAuthorTissue factor pathway inhibitor-
dc.subject.keywordAuthorXenotransplantation-
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