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

✍ Scribed by Yunel Perez; Aimara Valdivia; Leissy Gomez; Benjamin K. Simpson; Reynaldo Villalonga

Publisher: John Wiley and Sons
Year: 2005
Tongue: English
Weight: 159 KB
Volume: 5
Category: Article
ISSN: 1616-5187
DOI: 10.1002/mabi.200500139

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✦ Synopsis

Abstract

Summary: 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.
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## Abstract Catalase was chemically modified with a monoactivated dextran derivative having a carboxylate group at its reducing end residue. The modified enzyme retained 77% of its initial specific activity and was 3‐fold more resistant to tryptic degradation. The plasma half‐life time was increase