Thermodynamics and kinetics of the hydrolysis of the reactive-site peptide bond in pancreatic trypsin inhibitor (Kunitz) by Dermasterias imbricata trypsin 1
- 8 January 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (1) , 131-137
- https://doi.org/10.1021/bi00542a020
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
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- The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor. 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated InhibitorEuropean Journal of Biochemistry, 1978
- Kinetics of the Interaction of α‐Chymotrypsin with Trypsin Kallikrein Inhibitor (Kunitz) in Which the Reactive‐Site Peptide Bond Lys‐15–Ala‐16 is SplitEuropean Journal of Biochemistry, 1978
- By-product analogs for bovine carboxypeptidase BBiochemistry, 1978
- Hydrolysis-Resynthesis Equilibrium of the Lysine-15–Alanine-16 Peptide Bond in Bovine Trypsin Inhibitor (Kunitz)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1975
- CHROMATOGRAPHY OF TRYPSIN AND ITS DERIVATIVES - CHARACTERIZATION OF A NEW ACTIVE FORM OF BOVINE TRYPSIN1968
- CARBOXYPEPTIDASE-B .4. PURIFICATION AND CHARACTERIZATION OF THE PORCINE ENZYME1960