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 p...
Topics
- Amino Acid Sequence
- Base Sequence
- Chromatography, Gel
- DNA
- Electrophoresis, Polyacrylamide Gel
- Genes, Fungal
- Glycosylation
- Hemolysis
- Humans
- Molecular Sequence Data
- Mutation
- Plasmids