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Improved pharmacokinetics and stability properties of catalase by chemical glycosidation with end-group activated dextran

✍ Scribed by Reynaldo Villalonga; Aymara Valdivia; Yunel Pérez; Bertha Chongo


Publisher
John Wiley and Sons
Year
2006
Tongue
English
Weight
70 KB
Volume
102
Category
Article
ISSN
0021-8995

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✦ Synopsis


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 increased to 7.3‐fold after glycosidation. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 102: 4573–4576, 2006


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