The use of recombinant hemagglutinine protein of rinderpest virus in enzyme immunoassay

dc.contributor.authorBulut, H
dc.contributor.authorBolat, Y
dc.contributor.authorBulut, Y
dc.contributor.authorÖzdarendeli, A
dc.contributor.authorDoymaz, MZ
dc.date.accessioned2026-08-12T17:10:39Z
dc.date.issued2003
dc.departmentFırat Üniversitesi
dc.description.abstractIn this study, Rinderpest virus (RPV) recombinant hemagglutinine protein (rH) fused with protein A region of Staphylococcus aureus was expressed in Escherichia coli and purified by IgG affinity chromatography. rH protein was also used to establish enzyme immunoassay. Therefore, to prevent IgG binding to the protein A the wells coated with the rH proteins were blocked by human serum. Afterwards, RPV antigens were added to the wells to evaluate this assay. To this end, serum from mice immunized with RPV was used for EIA. Our data indicated that the rH protein fused with protein A of Staphylococcus aureus can be reliably used for enzyme immunoassays.
dc.identifier.endpage252
dc.identifier.issn1300-0128
dc.identifier.issue1
dc.identifier.orcid0000-0002-5811-2588
dc.identifier.scopus2-s2.0-0037224494
dc.identifier.scopusqualityQ3
dc.identifier.startpage249
dc.identifier.urihttps://hdl.handle.net/11508/50834
dc.identifier.volume27
dc.identifier.wosWOS:000181960400034
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isotr
dc.publisherTubitak Scientific & Technological Research Council Turkey
dc.relation.ispartofTurkish Journal of Veterinary & Animal Sciences
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WoS_20260511
dc.subjectRinderpest virus
dc.subjectrecombinant hemagglutinine protein
dc.subjectenzyme immunoassay
dc.titleThe use of recombinant hemagglutinine protein of rinderpest virus in enzyme immunoassay
dc.title.alternativeSi?ir vebasi virüsü rekombinant hemaglutinin proteininin enzim i?mmunoassayda kullanimi
dc.typeArticle

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