Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Lys77-plasmin
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference20 articles.
1. Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors
2. Catalytic properties of serine proteases. 2. Comparison between human urinary kallikrein and human urokinase, bovine .beta.-trypsin, bovine thrombin, and bovine .alpha.-chymotrypsin
3. Proteinase Action;Ascenzi,1984
4. Catalytic properties of human Lys77-plasmin. A comparative steady-state and pre-steady-state study
5. The refined crystal structure of bovine β-trypsin at 1·8 Å resolution
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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. Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin;Biochemistry;1993-02-01
5. Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Glu1-, Lys77-, Val442- and Val561-plasmin: a comparative study;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1990-08
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