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Pharmacokinetics and Stability Properties of Catalase Modified with Water‐Soluble Polysaccharides
Author(s) -
Valdivia Aymara,
Pérez Yunel,
Gómez Leissy,
Ramírez Hector L.,
Schacht Etienne H.,
Villalonga Reynaldo
Publication year - 2006
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.200600037
Subject(s) - chemistry , polysaccharide , enzyme , macromolecule , catalase , trypsin , pharmacokinetics , chromatography , biochemistry , mannan , proteolytic enzymes , thermal stability , organic chemistry , medicine
Bovine liver catalase (EC 1.11.1.6) was chemically modified with mannan, carboxymethylcellulose, and carboxymethylchitin. The enzyme retained about 48–97% of the initial specific activity after glycosidation with the polysaccharides. The prepared neoglycoenzyme was 1.9–5.7 fold more stable against the thermal inactivation processes at 55°C, in comparison with the native counterpart. Also, the modified enzyme was more resistant to proteolytic degradation with trypsin. Pharmacokinetics studies revealed higher plasma half‐life time for all the enzyme‐polymer preparations, but better results were achieved for the enzyme modified with the anionic macromolecules.