Article
Characterization of a nonglycosylated single chain urinary plasminogen activator secreted from yeast.
The Journal of biological chemistry - 15 Jan 1990
Melnick L M, Turner B G, Puma P, Price-Tillotson B, Salvato K A, Dumais D R, Moir D T, Broeze R J, Avgerinos G C
Abstract excerpt
Using site-directed mutagenesis, we have changed the asparagine in human single-chain urinary plasminogen activator (u-PA) at position 302 to an alanine. This alteration removes the only known amino acid residue glycosylated in the protein. The single-chain u-PA containing an alanine residue at position 302 instead of asparagine (scu-PA(N302A] cDNA gene was expressed in the yeast Saccharomyces cerevisiae....
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