Article
Involvement of aspartic and glutamic residues in kringle-2 of tissue-type plasminogen activator in lysine binding, fibrin binding and stimulation of activity as revealed by chemical modification and oligonucleotide-directed mutagenesis.
Protein engineering - 1 Dec 1990
Weening-Verhoeff E J, Quax P H, van Leeuwen R T, Rehberg E F, Marotti K R, Verheijen J H
Abstract excerpt
Modification of glutamic and aspartic acid residues of tissue-type plasminogen activator (t-PA) with 1-ethyl-3(3-dimethyl-aminopropyl)-carbodiimide leads to a decrease in affinity for lysine and fibrin, to a decrease of plasminogen activation activity in the presence of a fibrin mimic, but leaves...
Topics
- Amino Acid Sequence
- Aspartic Acid
- Base Sequence
- Ethyldimethylaminopropyl Carbodiimide
- Fibrin
- Glutamates
- Kinetics
- Lysine
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation