Kinetics of substrate reaction during irreversible modification of enzyme activity for enzymes involving two substrates
- 1 August 1987
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 127 (3) , 253-270
- https://doi.org/10.1016/s0022-5193(87)80106-6
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Determination of rate constant for the irreversible inhibition of acetylcholine esterase by continuously monitoring the substrate reaction in the presence of the inhibitorBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- A kinetic study of the irreversible inhibition of an enzyme measured in the presence of coupled enzymes. Fluorescein isothiocyanate as inhibitor of the adenosinetriphosphatase activity from sarcoplasmic reticulumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Reactivation Kineties of diethylphosphoryl acetylcholine esteraseEuropean Journal of Biochemistry, 1985
- Human liver cathepsin LBiochemical Journal, 1985
- In vivo significance of kinetic constants of protein proteinase inhibitorsBiochemical Medicine, 1984
- Theory and experimental method for determining individual kinetic constants of fast-acting, irreversible proteinase inhibitorsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Kinetics for the inhibition of acetylcholinesterase from the electric eel by some organophosphates and carbamatesEuropean Journal of Biochemistry, 1984
- Interaction of the (2S,3S)-Isomer of Bestatin with Yeast Aminopeptidase I. Kinetic and Binding StudiesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1984
- Covalent Labeling of Active SitesAdvances in Protein Chemistry, 1967
- Organophosphates and CarbamatesPublished by Elsevier ,1963