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. 1990 Apr 16;88(2):297-301.
doi: 10.1016/0378-1119(90)90048-v.

Secretion of N-glycosylated human recombinant interleukin-1 alpha in Saccharomyces cerevisiae

G P Livi  1 , A A Ferrara, R Roskin, P L Simon, P R Young
Affiliations

Secretion of N-glycosylated human recombinant interleukin-1 alpha in Saccharomyces cerevisiae

G P Livi et al. Gene. .

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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