Reversible inhibition of penicillinase by quinacillin: Evaluation of mechanisms involving two conformational states of the enzyme
- 1 June 1978
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 82 (3) , 951-956
- https://doi.org/10.1016/0006-291x(78)90875-6
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Preferential nitration with tetranitromethane of a specific tyrosine residue in penicillinase from Staphylococcus aureus PCl. Evidence that the preferentially nitrated residue is not part of the active site but that loss of activity is due to intermolecular cross-linkingBiochemical Journal, 1978
- The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studiesBiochemical Journal, 1976
- The amino acid sequence of Staphylococcus aureus penicillinaseBiochemical Journal, 1975
- The active site of penicillinase from Staphylococcus aureus PC1. Isolation of a specific covalent complex with the substrate quinacillinBiochemical Journal, 1975
- Some relationships between implicit Runge-Kutta, collocation and Lanczosτ methods, and their stability propertiesBIT Numerical Mathematics, 1970
- Substrate-specific inactivation of staphylococcal penicillinaseBiochemical Journal, 1967
- Quinacillin: A New Penicillin With Unusual PropertiesNature, 1963
- Statistical estimations in enzyme kineticsBiochemical Journal, 1961