SECRETION OF N-GLYCOSYLATED HUMAN RECOMBINANT INTERLEUKIN-1-ALPHA IN SACCHAROMYCES-CEREVISIAE

被引：26

作者：

LIVI, GP

FERRARA, A

ROSKIN, R

SIMON, PL

YOUNG, PR

机构：

[1] SMITHKLINE BEECHAM PHARMACEUT,DEPT IMMUNOL,KING OF PRUSSIA,PA 19406

[2] SMITHKLINE BEECHAM PHARMACEUT,DEPT MOLEC GENET,KING OF PRUSSIA,PA 19406

来源：

GENE | 1990年 / 88卷 / 02期

关键词：

endoglycosidase H; glyceraldehyde-6-phosphate dehydrogenase promoter; heterologous gene expression; human lymphokines; oligosaccharides; Recombinant DNA; yeast signal peptides;

D O I：

10.1016/0378-1119(90)90048-V

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

We have expressed fragments of the cDNA coding for mature human interleukin-1α(hIL-1α) in Saccharomyces cerevisiae. Mature hIL-1α 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-1α. The extent of glycosylation was significantly reduced using the α-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. © 1990.

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页码：297 / 301

页数：5

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