Study on Pegylation of Therapuetic Enzyme Uricase And Its Physio-Chemical Properties For Improving Its Pharmaceutical Characteristics
Author(s) -
Pooja Nanda,
P.E.Jagdeesh Babu
Publication year - 2013
Publication title -
international journal of pharmacology and pharmaceutical technology
Language(s) - English
Resource type - Journals
ISSN - 2277-3436
DOI - 10.47893/ijppt.2013.1010
Subject(s) - pegylation , urate oxidase , allantoin , chemistry , peg ratio , polyethylene glycol , uric acid , enzyme , conjugate , biochemistry , combinatorial chemistry , organic chemistry , mathematical analysis , mathematics , finance , economics
Uricase (urate oxidase EC 1.7.3.3, UC) catalyses t h oxidation of uric acid, a final product of purin e catabolism to allantoin. In the present work, Uricase is bioconju gated using PEG (Polyethylene glycol) as a chemical tool for linking for obtaining conjugates with better and desirable pharmaceutical properties. Uricase from Bacillus fastidisous (Uc) was modified through PEGylation considering various concentrations of li near polyethyleneglycol-8KDa (PEG-8K). The Uc-PEG 8 K conjugates, formed by conjugating Uc and PEG-8K in the ratio of 1:15 r etained 87.5% of the initial uricolytic activity, a nd were highly stable at pH 6.0, which is quiet close to physiological pH and at a t emperature of 16°C.
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