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 (SODCMCedac). The SOD-CMCox and SOD-CMCedac conjugates contained about 1.8–1.2mol 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 34.7h – 6.6h when compared with 4.8min for native SOD. The anti-inflammatory activity of the enzyme was 2–2.4 times increased after conjugation with the polymer.
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