Showing papers on "Acetylthiocholine published in 1982"

TL;DR: Steady-state kinetic studies were made on the very efficient enzyme hydrolysis of acetylthiocholine by electric eel acetylcholinesterase in glycerol/water solvents of increased viscosity, showing kmin, the very fast minimum substrate association rate constants, is as large or larger than plausible models for a simple diffusion-controlled reaction between a charged enzyme and substrate would suggest.

TL;DR: It is demonstrated that activation of the rate of acetylthiocholine hydrolysis in a low ionic strength medium is a rapid process and in this sense La3+ resembles other activating metal ions such as Ca2,+ and Mg2+.

TL;DR: A continuous spectrophotometric procedure is presented for the measurement of the kinetic properties of acetylcholinesterase with its natural substrate, acetyl choline, based upon the production of stoichiometric quantities of H+ upon hydrolysis of substrate.