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 instrument revealing the possibility of supramolecular structures formation, we have shown that the native alpha-chymotrypsin can form complexes with glycoproteins. Dimers of the native alpha-chymotrypsin with the artificially glycosylated one and with horseradish peroxidase (natural glycoprotein) were obtained. The position of the optimum on the dependence 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.