Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran.
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.
Valdivia
Aymara
A
Center for Enzyme Technology, University of Matanzas, Autopista a Varadero Km 3 1/2, Matanzas, C.P. 44740, Cuba.
Villalonga
Reynaldo
R
Di Pierro
Prospero
P
Pérez
Yunel
Y
Mariniello
Loredana
L
Gómez
Leissy
L
Porta
Raffaele
R
D000818:Animals; D002103:Cadaverine / Q000031:analogs & derivatives / Q000737:chemistry; D002374:Catalase / Q000097:blood / Q000737:chemistry* / Q000493:pharmacokinetics; D002384:Catalysis; D002417:Cattle; D003911:Dextrans / Q000737:chemistry* / Q000493:pharmacokinetics; D003959:Diamines / Q000737:chemistry; D005260:Female; D005456:Fluorescent Dyes / Q000737:chemistry; D051381:Rats; D017208:Rats, Wistar; D013302:Streptomyces / Q000201:enzymology; D011503:Transglutaminases / Q000737:chemistry*
D003911:Dextrans; D003959:Diamines; D005456:Fluorescent Dyes; D002374:Catalase; D011503:Transglutaminases; C008542:monodansylcadaverine; D002103:Cadaverine