期刊
JOURNAL OF BIOTECHNOLOGY
卷 122, 期 3, 页码 326-333出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2005.12.014
关键词
catalase; transglutaminase; dextran; pharmacokinetics
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 degrees 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. (c) 2006 Elsevier B.V. All rights reserved.
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