ARGININE MODIFICATION IN KUNITZ BOVINE TRYPSIN INHIBITOR THROUGH 1, 2-CYCLOHEXANEDIONE*
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 10 (2) , 146-152
- https://doi.org/10.1111/j.1399-3011.1977.tb02788.x
Abstract
Arginine residues (5.5 of 6) of the trypsin-kallikrein inhibitor from bovine organs (Kunitz inhibitor) were selectively modified by reaction with 1, 2-cyclohexanedione in sodium borate buffer, pH 9.0. The modified inhibitor is still highly active in inhibiting trypsin and chymotrypsin at 1:1 inhibitor:enzyme molar ratio and full inhibition was acheived at slightly higher molar ratio. The extent of correct refolding, on reoxidation of the reduced, arginine-modified inhibitor is diminished and regeneration of 2 arginines occurred under the reduction conditions. The stability constants and the standard-free energies of binding of the complexes between trypsin, or chymotrypsin, and the native, the arginine-modified and the reduced and reoxidized arginine-modified inhibitor have been determined from inhibitory assays.This publication has 35 references indexed in Scilit:
- Determination of Arginine in the Reactive Site of Proteinase Inhibitors by Selective and Reversible Derivatization of the Arginine Side ChainHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- The Reactive Sites of Kunitz Bovine‐Trypsin InhibitorEuropean Journal of Biochemistry, 1975
- Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolutionActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1975
- The Model of the Basic Pancreatic Trypsin Inhibitor Refined at 1.5 Å ResolutionPublished by Springer Nature ,1974
- A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsinJournal of Molecular Biology, 1972
- Structure and Mechanism of Action of a Pancreatic Trypsin InhibitorPublished by Elsevier ,1970
- On proteins. C. Disulfide bonds of basic trypsin inhibitor from beef pancreasCollection of Czechoslovak Chemical Communications, 1966
- Notizen: Zur Identität des Kallikrein-Inaktivators aus Rinderlunge und RinderparotisZeitschrift für Naturforschung B, 1965
- On proteins XCIV. Primary structure of basic trypsin inhibitor from beef pancreasCollection of Czechoslovak Chemical Communications, 1965
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959