Biomedical subjects
Publications and source records attributed to M Brufani.
The inhibition of eel acetylcholinesterase by physostigmine at 20 degrees and 25 degrees C have been investigated. In our evaluation the unimolecular reactivation rate constant, k3, the carbamylation rate constant, k2, and the binding constant, Ka, are the first simultaneously determined. The mechanism of this reaction is discussed.
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The authors, with a spectrophotometric procedure, have evaluated the kinetic constants of physostigmine, a cholinesterase inhibitor which assumes an important function when the degeneration of cholinergic projections is observed. This approach overcomes some of the difficulties encountered in measuring the binding and the carbamylation rate constants. A kinetic treatment, consistent with the experimental results observed in the enzyme-inhibitor system in the presence of substrate, is developed.