Pharmacokinetics and stability properties of catalase modified with water-soluble polysaccharides.
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 degrees 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.
Valdivia
Aymara
A
Center for Enzyme Technology, University of Matanzas, Matanzas, Cuba.
Pérez
Yunel
Y
Gómez
Leissy
L
Ramírez
Hector L
HL
Schacht
Etienne H
EH
Villalonga
Reynaldo
R
D000818:Animals; D019540:Area Under Curve; D002240:Carbohydrate Sequence; D002266:Carboxymethylcellulose Sodium / Q000737:chemistry / Q000378:metabolism; D002374:Catalase / Q000008:administration & dosage / Q000737:chemistry / Q000493:pharmacokinetics*; D002417:Cattle; D004795:Enzyme Stability; D006207:Half-Life; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007275:Injections, Intravenous; D008099:Liver / Q000201:enzymology; D008297:Male; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011134:Polysaccharides / Q000737:chemistry*; D051381:Rats; D017208:Rats, Wistar; D012995:Solubility; D013053:Spectrophotometry; D013379:Substrate Specificity; D014867:Water / Q000737:chemistry
D011134:Polysaccharides; D014867:Water; D002374:Catalase; D002266:Carboxymethylcellulose Sodium