LECTIN-LIKE CENTER IN THE MOLECULE OF ALPHA-CHYMOTRYPSIN - FORMATION OF COMPLEXES WITH PEROXIDASE AND ARTIFICIALLY GLYCOSYLATED ALPHA-CHYMOTRYPSIN

Using the system of reversed micelles of Aerosol OT1 in octane as an i nstrument revealing the possibility of supramolecular structures forma tion, we have shown that the native alpha-chymotrypsin can form comple xes with glycoproteins. Dimers of the native alpha-chymotrypsin with t he artificially glycosylated one and with horseradish peroxidase (natu ral glycoprotein) were obtained. The position of the optimum on the de pendence of the catalytic activity upon the hydration degree confirms the compact organization of the formed complexes. The ability of alpha -chymotrypsin to form such kind of complexes seems to play a key role in its absorption on glycocalix in vivo.