Fluorescence polarization studies on the interaction of active site modified chymotrypsins with .alpha.1-protease inhibitor
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00532a022
Reference37 articles.
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2. Soybean trypsin inhibitor (Kunitz) and its complex with trypsin. Carbon-13 nuclear magnetic resonance studies of the reactive site arginine
3. Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin.
4. A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin
5. Investigations of the Chymotrypsin-catalyzed Hydrolysis of Specific Substrates
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3. Change in Environment of the P1 Side Chain upon Progression from the Michaelis Complex to the Covalent Serpin−Proteinase Complex;Biochemistry;1998-09-01
4. Apparent Formation of Sodium Dodecyl Sulfate-stable Complexes between Serpins and 3,4-Dichloroisocoumarin-inactivated Proteinases Is Due to Regeneration of Active Proteinase from the Inactivated Enzyme;Journal of Biological Chemistry;1997-05
5. Role of the Catalytic Serine in the Interactions of Serine Proteinases with Protein Inhibitors of the Serpin Family;Journal of Biological Chemistry;1995-12
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