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dc.contributor.authorPorntip Laummaunwaien_US
dc.contributor.authorPewpan M. Intapanen_US
dc.contributor.authorChaisiri Wongkhamen_US
dc.contributor.authorViraphong Lulitanonden_US
dc.contributor.authorChatchai Tayapiwatanaen_US
dc.contributor.authorWanchai Maleewongen_US
dc.date.accessioned2018-09-04T04:47:26Z-
dc.date.available2018-09-04T04:47:26Z-
dc.date.issued2010-12-01en_US
dc.identifier.issn10902449en_US
dc.identifier.issn00144894en_US
dc.identifier.other2-s2.0-80054913334en_US
dc.identifier.other10.1016/j.exppara.2010.06.004en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=80054913334&origin=inwarden_US
dc.identifier.urihttp://cmuir.cmu.ac.th/jspui/handle/6653943832/50912-
dc.description.abstractIn this study, a cDNA encoding cyclophilin (CyP) of Gnathostoma spinigerum was cloned into a prokaryotic expression vector and expressed in Escherichia coli. The predicted molecular mass of the putative protein was 18.6. kDa, and the deduced amino acid sequence had 86, 84.8, 81.3 and 77.2% identity with the CyP of Dirofilaria immitis, Brugia malayi, Onchocerca volvulus and Caenorhabditis elegans, respectively. A prediction of linear B-cell epitopes with high hydrophilicity and immunoblotting results indicated that the recombinant CyP has antigenicity to humans. The recombinant CyP protein reacted with human gnathostomiasis sera but not with other parasitosis or healthy control sera, suggesting that it might be useful for the serodiagnosis of human gnathostomiasis. © Elsevier Inc.en_US
dc.subjectImmunology and Microbiologyen_US
dc.subjectMedicineen_US
dc.titleGnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin proteinen_US
dc.typeJournalen_US
article.title.sourcetitleExperimental Parasitologyen_US
article.volume126en_US
article.stream.affiliationsKhon Kaen Universityen_US
article.stream.affiliationsChiang Mai Universityen_US
Appears in Collections:CMUL: Journal Articles

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