[Age changes in the allosteric properties of brain acetylcholinesterase].

d-tubocurarine and procaine have been shown to inhibit the acetylcholinesterase of rat brain homogenate by coupled and non-competitive mechanism respectively, which suggests binding to enzyme peripheral sites. Judging by values of Hill coefficient negative cooperativity in interactions between procaine sites is characteristic of all ages (n=0,8 and 0,53 for young and old rats) while such cooperativity for d-tubocurarine sites appears only at old age (n=1 and 0,6 for young and old animals). Values of Ki changed in opposite directions for each of the substances with aging.

[Comparative study of membrane-bound acetylcholinesterase in guinea pig and rabbit brains].

As a result of kinetic studies on acetylcholinesterase inhibition by allosteric effector d-tubocurarine it was shown that interaction between modifier and catalytic sites of rabbit and guinea pig acetylcholinesterase are different for these two species. Judging by the inhibition curves and sensitivity of d-tubocurarine theses differences involve enzyme microenvironment in the membrane. Addition to 7,15-10-6 M d-tubocurarune to solubilized preparation led to a significant fall in the value of Hill coefficient for enzyme-substrate interaction.