Article
The N-terminal domain of antithrombin-III is essential for heparin binding and complex-formation with, but not cleavage by, alpha-thrombin.
The Biochemical journal - 1 Mar 1992
Austin R C, Sheffield W P, Rachubinski R A, Blajchman M A
Abstract excerpt
Normal and mutant forms of human antithrombin-III (AT-III) were synthesized in a cell-free system in order to identify putative functional domains required for heparin binding and complex-formation with alpha-thrombin. Heparin-Sepharose chromatography resulted in the elution of approx. 70% of cell-free-derived normal AT-III-(1-432)-polypeptide as a peak between 0.2 M- and 0.7 M-NaCl. The cell-free-derived normal...
Topics
- Antithrombin III
- Base Sequence
- Cell-Free System
- Chromatography, Gel
- DNA
- Disulfides
- Electrophoresis, Polyacrylamide Gel
- Gene Expression
- Heparin
- Humans
- Molecular Sequence Data