Key result
Sequential deletions of the positively charged C-terminus of TFPI decreased inhibitory activity against factor Xa and affinity for heparin-agarose.
Population
In vitro biochemical assays using human factor Xa and bovine γ-carboxyglutamate (Gla)-domainless factor Xa
Comparison
Altered forms of recombinant tissue factor… vs Full-length rTFPI and varying assay conditions
Design
Preclinical
Authors
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C-terminal integrity of TFPI supports optimal factor Xa inhibition in vitro; leaves open any therapeutic targeting in coagulation disorders.
The C-terminal polypeptide of TFPI, including part of the third Kunitz-type domain, is essential for heparin binding and optimal factor Xa inhibition in the presence of calcium and phospholipids.
Wesselschmidt et al. (1993) studied this question. Altered forms of recombinant TFPI (rTFPI) vs. Full-length rTFPI was evaluated on Inhibition of factor Xa and heparin binding. Sequential deletions of the positively charged C-terminus of TFPI decreased inhibitory activity against factor Xa and affinity for heparin-agarose.
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