[Activity of membrane-bound acetylcholinesterases in the presence of benzene alcohol and concanavalin A].

UV-sensitivity of membrane-bound acetylcholinesterases in the presence of agents, which selectively modify lipid phase and integral proteins of erythrocytic membranes (benzene alcohol and concanavalin A), has been studied. It has been determined, that UV-irradiation of human erythrocytic membranes within the range of wavelengths 240-390 and 300-400 nm leads to differently directed changes of enzymatic activity, which are caused by different number of membranous chromophores of UV-light and by their different nature. The scheme of process, causing the photomodification of membranous acetylcholinesterases, has been suggested. It takes into consideration a contribution of several structural components of membranes in these processes. Authors have made the conclusion about the important role of microenvironment in processes of acetylcholinesterases functioning and about the possibility of purposeful regulation of its UV-sensitivity by introduction of exogenous agents, which modify structural state of closest "neighbours" of enzyme.