Secretion of N-glycosylated human recombinant interleukin-1 alpha in Saccharomyces cerevisiae |
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Authors: | G P Livi A A Ferrara R Roskin P L Simon P R Young |
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Institution: | Department of Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406-0939. |
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Abstract: | We have expressed fragments of the cDNA coding for mature human interleukin-1 alpha (hIL-1 alpha) in Saccharomyces cerevisiae. Mature hIL-1 alpha contains one potential N-linked glycosylation site that is not recognized in mammalian cells. Translational fusions to either one of three yeast signal sequences resulted in secretion of bioactive, N-glycosylated hIL-1 alpha. The extent of glycosylation was significantly reduced using the alpha-factor signal sequence, which itself contains three N-linked glycosylation sites known to be core glycosylated. N-glycosylation has no effect on biological specific activity. |
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