Transformation of active-site lysine in naturally occurring trypsin inhibitors. A basis for a general mechanism for inhibition of proteolytic enzymes
- 1 August 1968
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 7 (8) , 2879-2885
- https://doi.org/10.1021/bi00848a026
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Peptide Bond Cleavage on Trypsin-Trypsin Inhibitor Complex FormationJournal of Biological Chemistry, 1965
- Kinetics and mechanism of catalysis by proteolytic enzymes. 2. Kinetic studies of thrombin-catalysed reactions and their modification by bile salts and other detergentsBiochemical Journal, 1964
- The kinetics of hydrolysis of derivatives of arginine, homoarginine and ornithine by trypsinBiochemical Journal, 1964
- Chemical Modification of Avian Ovomucoids*Biochemistry, 1963
- Properties of Chromatographically Purified Trypsin Inhibitors from Lima BeansBiochemistry, 1963
- Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association*Biochemistry, 1962
- A MODIFIED SPECTROPHOTOMETRIC DETERMINATION OF CHYMOTRYPSIN, TRYPSIN, AND THROMBINCanadian Journal of Biochemistry and Physiology, 1959
- Preparation and Properties of Guanidinated MercuripapainJournal of Biological Chemistry, 1959
- Kinetics of the reaction between trypsin and the pancreatic trypsin inhibitorBiochemical Journal, 1957
- Influence du calcium sur la stabilité du complexe trypsine-ovomucoïdeBiochimica et Biophysica Acta, 1952