Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran |
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Authors: | Valdivia Aymara Villalonga Reynaldo Di Pierro Prospero Pérez Yunel Mariniello Loredana Gómez Leissy Porta Raffaele |
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Affiliation: | Center for Enzyme Technology, University of Matanzas, Autopista a Varadero Km 3 1/2, Matanzas, C.P. 44740, Cuba. |
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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 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. |
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