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Improved Pharmacokinetics Properties for Catalase by Site‐Specific Glycosidation with Aminated Dextran
Author(s) -
Pérez Yunel,
Valdivia Aymara,
Ramírez Hector L.,
Villalonga Reynaldo
Publication year - 2005
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/marc.200500291
Subject(s) - conjugate , catalase , dextran , carbodiimide , chemistry , pharmacokinetics , enzyme , biochemistry , pharmacology , biology , mathematical analysis , mathematics
Summary: Catalase was chemically modified with an end‐group aminated dextran derivative via a carbodiimide catalyzed reaction. The enzymatic activity of catalase was increased after glycosidation with 4 mol of polymer. This modification improved the pharmacokinetic behavior of catalase, increasing by 7.8‐ and 20‐fold the plasma half‐life times for the α and β phases, and reducing by 176‐fold the total clearance after intravenous administration in rats.Schematic of the catalase dextran conjugate synthesized here.