Expression of a functional human interleukin-18 in yeast

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dc.contributor.authorY Y Lim-
dc.contributor.authorM Y Lee-
dc.contributor.authorB W Chung-
dc.contributor.authorS M Park-
dc.contributor.authorSung Goo Park-
dc.contributor.authorY S Jang-
dc.contributor.authorM S Yang-
dc.contributor.authorD H Kim-
dc.date.accessioned2017-04-19T08:59:29Z-
dc.date.available2017-04-19T08:59:29Z-
dc.date.issued2002-
dc.identifier.issn01410229-
dc.identifier.uri10.1016/S0141-0229(02)00043-1ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6000-
dc.description.abstractThe cDNA sequence for mature human interleukin-18 gene (hIL-18) was cloned and then used to transform Saccharomyces cerevisiae. Two different promoters for heterologous expression of hIL-18 were tested: glyceraldehyde-3-phosphate dehydrogenase (GPD) promoter and a yeast hybrid ADH2-GPD promoter consisting of alcohol dehydrogenase II (ADH2) and GPD promoter. Northern blot analysis revealed that, although variation in the expression level of rhIL-18 existed among transformants, the highest expression was obtained by the GPD promoter. Expressed hIL-18 protein (rhIL-18) was successfully secreted into culture medium due to the presence of the signal peptide of rice amylase 1A. It was possible to produce 13 mg of rhIL-18 protein per liter of culture filtrate without any changes in cell growth. Both cell growth and rhIL-18 production reached the peaks after the 3-day cultivation while the accumulation of transgene transcript peaked at 24 h of cultivation. The secreted rhIL-18 had an estimated molecular mass of 18 kDa. The bioassay observing the induction of interferon-γ from the KG-1 cell line indicated that the secreted recombinant rhIL-18 was bioactive and the specific activity of yeast-derived rhIL-18 was enhanced 15 times relative to that of E. coli-derived rhIL-18.-
dc.publisherElsevier-
dc.titleExpression of a functional human interleukin-18 in yeast-
dc.title.alternativeExpression of a functional human interleukin-18 in yeast-
dc.typeArticle-
dc.citation.titleEnzyme and Microbial Technology-
dc.citation.number6-
dc.citation.endPage709-
dc.citation.startPage703-
dc.citation.volume30-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName임영이-
dc.contributor.alternativeName이미예-
dc.contributor.alternativeName정봉우-
dc.contributor.alternativeName박승문-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName장용석-
dc.contributor.alternativeName양문식-
dc.contributor.alternativeName김대혁-
dc.identifier.bibliographicCitationEnzyme and Microbial Technology, vol. 30, no. 6, pp. 703-709-
dc.identifier.doi10.1016/S0141-0229(02)00043-1-
dc.subject.keywordHuman interleukin 18-
dc.subject.keywordSaccharomyces cerevisiae-
dc.subject.localHuman interleukin 18-
dc.subject.localSaccharomyces cerevisiae-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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