Binding of the Bovine Basic Pancreatic Trypsin Inhibitor (Kunitz Inhibitor) to Human and Bovine Factor Xa. A Thermodynamic Study
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm3.1990.371.1.389/pdf
Reference13 articles.
1. Blood Coagulation
2. COFACTOR PROTEINS IN THE ASSEMBLY AND EXPRESSION OF BLOOD CLOTTING ENZYME COMPLEXES
3. Kunitz-type inhibitors in human serum. Identification and characterization.
4. Active site of bovine factor Xa. Characterization using substituted benzamidines as competitive inhibitors and affinity-labeling reagents.
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1. Binding of recombinant PrPc to human plasminogen: Kinetic and thermodynamic study using a resonant mirror biosensor;Proteins: Structure, Function, and Bioinformatics;2004-12-17
2. Kinetic and equilibrium characterization of the interaction between bovine trypsin and I-ovalbumin;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2004-11
3. The Bovine Basic Pancreatic Trypsin Inhibitor (Kunitz Inhibitor): A Milestone Protein;Current Protein & Peptide Science;2003-06-01
4. Serine proteinase inhibition by the active site titrant N α-(N,N-dimethylcarbamoyl)-α-azaornithine p-nitrophenyl ester;European Journal of Biochemistry;2000-02
5. Aprotinin, the First Competitive Protein Inhibitor of NOS Activity;Biochemical and Biophysical Research Communications;1998-08
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