Glycosidation of Cu,Zn-Superoxide Dismutase with End-Group Aminated Dextran. Pharmacological and Pharmacokinetics Properties

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...

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Veröffentlicht in:	Macromolecular bioscience 2005-12, Vol.5 (12), p.1220-1225
Hauptverfasser:	Perez, Yunel, Valdivia, Aimara, Gomez, Leissy, Simpson, Benjamin K., Villalonga, Reynaldo
Format:	Artikel
Sprache:	eng
Schlagworte:	Amines - chemistry Animals anti-inflammatory Anti-Inflammatory Agents, Non-Steroidal - pharmacology Applied sciences Area Under Curve Aspartic Acid - chemistry Biological and medical sciences Carbohydrate Sequence dextran Dextrans - chemistry Edema - drug therapy Enzyme Activation Exact sciences and technology Foot Diseases - drug therapy General pharmacology Glucosides - metabolism Glutamic Acid - chemistry Half-Life Male Medical sciences modified enzymes Molecular Sequence Data Natural polymers Pharmaceutical technology. Pharmaceutical industry pharmacokinetics Pharmacology. Drug treatments Physicochemistry of polymers Rats Rats, Wistar Starch and polysaccharides superoxide dismutase Superoxide Dismutase - chemistry Superoxide Dismutase - metabolism Superoxide Dismutase - pharmacology
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Zusammenfassung:	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.
ISSN:	1616-5187 1616-5195
DOI:	10.1002/mabi.200500139