Glycosidation of Cu,Zn-superoxide dismutase with end-group aminated dextran. Pharmacological and pharmacokinetics properties

Abstract

Bovine Cu,Zn-SOD was chemically modified with an end-group aminated dextran derivative using a water-soluble carbodiimide as coupling agent. The enzyme retained 81% of the initial catalytic activity after the attachment of about 4.4 mol of polymer per protein subunit. The anti-inflammatory activity of the SOD was two times increased after conjugation with dextran. The modified enzyme was remarkably more resistant to inactivation by H2O2 and its plasma half-life time was prolonged from 4 min to 3.2 h. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.