RESUMO
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 H(2)O(2) and its plasma half-life time was prolonged from 4 min to 3.2 h.
Assuntos
Dextranos/química , Superóxido Dismutase/química , Superóxido Dismutase/farmacologia , Aminas/química , Animais , Anti-Inflamatórios não Esteroides/farmacologia , Área Sob a Curva , Ácido Aspártico/química , Sequência de Carboidratos , Edema/tratamento farmacológico , Ativação Enzimática , Doenças do Pé/tratamento farmacológico , Glucosídeos/metabolismo , Ácido Glutâmico/química , Meia-Vida , Masculino , Dados de Sequência Molecular , Ratos , Ratos Wistar , Superóxido Dismutase/metabolismoRESUMO
O-carboxymethylchitin (molecular weight = 1.07 x 10(5), degree of carboxymethylation = 80%, degree of N-acetylation = 91%) was chemically attached to superoxide dismutase by the formation of amide linkages through a carbodiimide catalyzed reaction. The glycosidated enzyme contained about 1.8 mole of polysaccharide per mole of protein and retained 57% of the initial catalytic activity. The anti-inflammatory activity of the enzyme was 2.4 times increased after conjugation with the polysaccharide. The modified superoxide dismutase preparation was remarkably more resistant to inactivation with H(2)O(2) and its plasma half-life time was prolonged from 4.8 min to 69 h.
