Article
Tissue-type plasminogen activator mutants imitating urokinase in the peptide link between kringle and protease domains and at selected sites within the protease domain.
European journal of biochemistry - 1 Apr 1993
Hinzmann B, Wernicke D, Pfeifer M, Zacharias U, Fischer B, Eisenmenger F, Will H
Abstract excerpt
Tissue-type plasminogen activator (tPA) mutants which, at selected amino acid positions, mimic urokinase-type plasminogen activator (uPA) were expressed in Chinese hamster ovary cells and examined for their catalytic properties. In one series of mutants, the dipeptide Ser262 Thr263 between kringle 2 and the protease domain of tPA was (a) replaced by an Ala residue, (b) lengthened by additional Ser and Ala...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- CHO Cells
- Cloning, Molecular
- Cricetinae
- DNA
- Endopeptidases
- Humans
- Kinetics
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Sequence Homology, Amino Acid