Improved anti-inflammatory and pharmacokinetic properties for superoxide dismutase by chemical glycosidation with carboxymethylchitin.

Abstract:

: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.

journal_name

Macromol Biosci

authors

Valdivia A,Perez Y,Dominguez A,Caballero J,Gomez L,Schacht EH,Villalonga R

doi

10.1002/mabi.200400114

subject

Has Abstract

pub_date

2005-02-23 00:00:00

pages

118-23

issue

2

eissn

1616-5187

issn

1616-5195

journal_volume

5

pub_type

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