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Improved pharmacokinetics and stability properties of catalase by chemical glycosidation with end‐group activated dextran
Author(s) -
Villalonga Reynaldo,
Valdivia Aymara,
Pérez Yunel,
Chongo Bertha
Publication year - 2006
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.25019
Subject(s) - dextran , residue (chemistry) , chemistry , catalase , enzyme , carboxylate , derivative (finance) , chemical modification , chemical stability , chromatography , organic chemistry , polymer chemistry , financial economics , economics
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