Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/55286
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSophit Khanthawongen_US
dc.contributor.authorNongnuch Vanittanakomen_US
dc.date.accessioned2018-09-05T02:54:00Z-
dc.date.available2018-09-05T02:54:00Z-
dc.date.issued2016-01-01en_US
dc.identifier.issn01252526en_US
dc.identifier.other2-s2.0-84961829784en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84961829784&origin=inwarden_US
dc.identifier.urihttp://cmuir.cmu.ac.th/jspui/handle/6653943832/55286-
dc.description.abstract© 2016, Chiang Mai University. All Rights reserved. Talaromyces (Penicillium) marneffei is a thermal dimorphic fungus that can cause a fatal disseminated disease in human immunodeficiency virus-infected patients. The routes of infection and factors that affect the pathogenicity of this fungus remain unclear. The previous studies demonstrated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an adherence factor in T. marneffei during early phase of infection. In this study, recombinant GAPDH of T. marneffei was produced in a eukaryotic expression system, Pichia pastoris. The full-length gpdA gene of T. marneffei was amplified from cDNA clones using primers with restriction sequences. Then the amplified fragments were cloned into pPICzA plasmid and transformed into TOP10 E. coli competent cells. The fusion plasmids were purified, linearized and subsequently transformed into P. pastoris X-33 competent yeast cells by electroporation. The positive clones were then checked with PCR and sequencing. The selected clone was cultured and induced for recombinant protein expression. After purification, proteins of approximately 34 and 37 kDa were detected by coomassie blue stained gel. Only 37-kDa rGAPDH was identified by using western blot to detect his-tag. The rGAPDH was purified by using Ni-NTA reducing condition to remove the protein contamination. We have successfully cloned and produced GAPDH recombinant protein of T. marneffei in a yeast expression system. This protein will be further characterized for its virulence property.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemistryen_US
dc.subjectMaterials Scienceen_US
dc.subjectMathematicsen_US
dc.subjectPhysics and Astronomyen_US
dc.titleProduction of talaromyces (Penicillium) marneffei glyceraldehyde-3-phosphate dehydrogenase recombinant protein expressed by pichia pastorisen_US
dc.typeJournalen_US
article.title.sourcetitleChiang Mai Journal of Scienceen_US
article.volume43en_US
article.stream.affiliationsNaresuan Universityen_US
article.stream.affiliationsChiang Mai Universityen_US
Appears in Collections:CMUL: Journal Articles

Files in This Item:
There are no files associated with this item.


Items in CMUIR are protected by copyright, with all rights reserved, unless otherwise indicated.