Abstract

Superoxide dismutase (SOD) was chemically modified with carboxymethylcellulose through two different synthetic procedures: Reductive alkylation with the periodate-oxidized polymer (SOD-CMCox), and the formation of amide linkages through a carbodiimide catalyzed reaction (SOD-CMCedac). The SOD-CMCox and SOD-CMCedac conjugates contained about 1.8-1.2 mol of polymer per mol of protein, and retained 68-78% of the initial catalytic activity, respectively. The glycosidated enzymes were more resistant to inactivation with H2O2 and their plasma half-life times were prolonged to 34.7 h-6.6 h when compared with 4.8 min for native SOD. The anti-inflammatory activity of the enzyme was 2-2.4 times increased after conjugation with the polymer.