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Improved Anti-Inflammatory and Pharmacokinetic Properties for Superoxide Dismutase by Chemical Glycosidation with Carboxymethylchitin

✍ Scribed by Aimara Valdivia; Yunel Perez; Amalia Dominguez; Julio Caballero; Leissy Gomez; Etienne H. Schacht; Reynaldo Villalonga

Publisher: John Wiley and Sons
Year: 2005
Tongue: English
Weight: 114 KB
Volume: 5
Category: Article
ISSN: 1616-5187
DOI: 10.1002/mabi.200400114

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✦ Synopsis

Abstract

Summary: O‐Carboxymethylchitin (molecular weight = 1.07 × 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.

Superoxide dismutase‐O‐carboxymethylchitin conjugate.

magnified imageSuperoxide dismutase‐O‐carboxymethylchitin conjugate.

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