Abstract
A comparative study of native and artificially glycosylated α-chymotrypsin in reversed micelles of Aerosol OT in octane was carried out. d-Glucosamine and 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide were used as modifying agents to yield glycosylated enzyme. Unlike the native α-chymotrypsin, the modified protein tended to form reversible oligomeric structures, revealed by the appearance of an additional maximum (characteristic of dimeric forms of protein functioning) as a result of the enzyme catalytic activity being dependent on the AOT hydration degree. Dependence of the enzyme catalytic activity on the surfactant concentration in the case of the modified enzyme was similar to that of glycoproteins, and suggests its membrane affinity. The role of carbohydrate moieties in the functioning of glycoproteins is discussed.
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