Arginine modification in elastase. Effect on catalytic activity and conformation of the calcium-binding site.
Open Access
- 1 March 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (6) , 3851-3857
- https://doi.org/10.1016/s0021-9258(17)43175-9
Abstract
No abstract availableThis publication has 39 references indexed in Scilit:
- Modification of arginine residues in subtilisins Novo and CarlsbergInternational Journal of Peptide and Protein Research, 1983
- Crystallographic study of the binding of a trifluoroacetyl dipeptide anilide inhibitor with elastaseJournal of Molecular Biology, 1982
- Presence of an essential arginyl residue in D-β-hydroxybutyrate dehydrogenase from mitochondrial inner membraneBiochemical and Biophysical Research Communications, 1980
- Lanthanide probes in biological systems: the calcium binding site of pancreatic elastase as studied by terbium luminescenceBiochemistry, 1980
- Structure-function relations and site of action of apamin, a neurotoxic polypeptide of bee venom with an action on the central nervous systemBiochemistry, 1975
- Modification of Arginyl Residues in Porcine Carboxypeptidase BEuropean Journal of Biochemistry, 1975
- The active site of porcine elastaseJournal of Molecular Biology, 1975
- The synthesis and analytical use of a highly sensitive and convenient substrate of elastaseBiochemical Medicine, 1974
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Atomic coordinates for tosyl-elastaseBiochemical and Biophysical Research Communications, 1973