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dc.contributor.authorVirapong Prachayasittikulen_US
dc.contributor.authorChartchalerm Isarankura Na Ayudhyaen_US
dc.contributor.authorTheeraphon Piachamen_US
dc.contributor.authorRachada Kiatfuengfooen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-07-24T03:27:45Z-
dc.date.available2018-07-24T03:27:45Z-
dc.date.issued2003-12-01en_US
dc.identifier.citationAsian Pacific Journal of Allergy and Immunology. Vol.21, No.4 (2003), 259-267en_US
dc.identifier.issn0125877Xen_US
dc.identifier.other2-s2.0-2942566109en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=2942566109&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/20968-
dc.description.abstractGene fusion technique was successfully applied as a potential approach to create a metal-binding site to assist one-step purification of green fluorescent protein (GFP). The chimeric GFP carrying hexapolyhistidine (H6GFPuv) was purified to homogeneous protein via the Immobilized Metal Affinity Chromatography charged with zinc ions. Removal of metal tagger could readily be performed by using enterokinase enzyme. Engineering of the hexahistidine and enterokinase cleavage sites (DDDDK) onto the chimeric protein did not significantly affect the fluorescent property and the binding avidity to Burkholderia pseudomallei protease of a chimeric protease-binding GFP (H6PBGFPuv). This concludes that engineering of repetitive histidine regions onto interested target protein along with the enterokinase cleavage sites will ease the complication of protein purification.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=2942566109&origin=inwarden_US
dc.subjectMedicineen_US
dc.titleOne-step purification of chimeric green fluorescent protein providing metal-binding avidity and protease recognition sequenceen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
Appears in Collections:Scopus 2001-2005

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