The reversible deactivation of β-lactamase from Staphylococcus aureus by quinacillin and cephaloridine and its modification by antibodies
- 1 March 1984
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 785 (3), 104-110
- https://doi.org/10.1016/0167-4838(84)90133-x
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Inactivation of the RTEM .beta.-lactamase from Escherichia coli. Interaction of penam sulfones with the enzymeBiochemistry, 1981
- Inhibition of the RTEM .beta.-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acidBiochemistry, 1981
- Reversible inhibition of penicillinase by quinacillin: Evaluation of mechanisms involving two conformational states of the enzymeBiochemical and Biophysical Research Communications, 1978
- Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acidBiochemistry, 1978
- Active fragments obtained by cyanogen bromide cleavage of ovomucoidBiochemical Journal, 1976
- 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 formation and stabilization of protein structureBiochemical Journal, 1972
- PURIFICATION AND PROPERTIES OF THE EXOPENICILLINASE FROM STAPHYLOCOCCUS AUREUSBiochemical Journal, 1963
- Quinacillin: A New Penicillin With Unusual PropertiesNature, 1963