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Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran

Paper ID Volume ID Publish Year Pages File Format Full-Text
25500 43577 2006 8 PDF Available
Title
Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran
Abstract

An enzymatic approach, based on a transglutaminase-catalyzed coupling reaction, was investigated to modify bovine liver catalase with an end-group aminated dextran derivative. We demonstrated that catalase activity increased after enzymatic glycosidation and that the conjugate was 3.8-fold more stable to thermal inactivation at 55 °C and 2-fold more resistant to proteolytic degradation by trypsin. Moreover, the transglutaminase-mediated modification also improved the pharmacokinetics behavior of catalase, increasing 2.5-fold its plasma half-life time and reducing 3-fold the total clearance after its i.v. administration in rats.

Keywords
Catalase; Transglutaminase; Dextran; Pharmacokinetics
First Page Preview
Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 122, Issue 3, 10 April 2006, Pages 326–333
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering