Ionization Behavior of the Histidine Residue in the Catalytic Triad of Serine Proteases
Open Access
- 1 December 1973
- journal article
- Published by Elsevier
- Vol. 248 (23) , 8306-8308
- https://doi.org/10.1016/s0021-9258(19)43228-6
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- The charge relay system in chymotrypsin and chymotrypsinogenJournal of Molecular Biology, 1973
- A competitive labelling method for determining the ionization constants and reactivity of individual histidine residues in proteins. The histidines of α-chymotrypsinBiochemical Journal, 1972
- High resolution nuclear magnetic resonance study of the histidine—Aspartate hydrogen bond in chymotrypsin and chymotrypsinogenJournal of Molecular Biology, 1972
- Primary Structure of α-Lytic Protease: a Bacterial Homologue of the Pancreatic Serine ProteasesNature, 1970
- A comparison of properties of the α-lytic protease of Sorangium sp. and porcine elastaseCanadian Journal of Biochemistry, 1970
- [43] The α-lytic protease of a myxobacteriumPublished by Elsevier ,1970
- Kinetic properties of the α-lytic protease of Sorangium sp., a bacterial homologue of the pancreatopeptidasesCanadian Journal of Biochemistry, 1969
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969
- CONCERNING THE NATURE OF THE α- AND β-LYTIC PROTEASES OF SORANGIUM SP.Canadian Journal of Biochemistry, 1967
- Three-dimensional Structure of Tosyl-α-chymotrypsinNature, 1967