Amalia Domínguez

Improved Pharmacological Properties for Superoxide Dismutase Modified with Carboxymethycellulose

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.

Improved pharmacological properties for superoxide dismutase modified with mannan

Mannan from Sacharomyces cerevisiae was activated by oxidation with NaIO4 (sodium m‐periodate) and further linked to SOD (superoxide dismutase) via reductive alkylation with NaBH4 (sodium borohydride). The gly‐cosidated enzyme contained an average of 1.2 mol of polysaccharide per mol of protein and retained 52% of its initial activity. The modified enzyme was 560‐fold more resistant to inactivation with H2O2 and acquired a lectin‐recognition capacity in respect of concanavalin A. The anti‐inflammatory activity of SOD was increased 2‐fold and its plasma half‐life time was prolonged from 4.8 min to 1.7 h after glycosylation with the polymer.