| Literature DB >> 3311885 |
V Price1, D Mochizuki, C J March, D Cosman, M C Deeley, R Klinke, W Clevenger, S Gillis, P Baker, D Urdal.
Abstract
Expression and secretion of two lymphokines, murine granulocyte-macrophage colony-stimulating factor (MuGM-CSF) and bovine interleukin-2 (BoIL-2), to levels of 50-60 mg per liter were achieved by placing these cDNAs in a Saccharomyces cerevisiae expression vector that utilized the yeast alcohol dehydrogenase-2 promoter and alpha-factor leader peptide. These lymphokines were purified to homogeneity by direct application of the crude yeast medium to reversed-phase high-performance liquid chromatography. Despite the fact that both lymphokines contain at least one N-glycosylation site and have identical N-terminal residues (Ala-Pro-Thr), recombinant (R) GM-CSF was found to be heterogeneously glycosylated by yeast while RBoIL-2 was secreted without glycosylation. Additionally, approximately 40% of the RGM-CSF was found to be proteolytically cleaved after the second amino acid residue, while RBoIL-2 was found to be intact.Entities:
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Year: 1987 PMID： 3311885 DOI： 10.1016/0378-1119(87)90288-5
Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688