Improved Pharmacological Properties for Superoxide Dismutase Modified with Carboxymethycellulose
Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, Autopista a Varadero Km 3 1/2, Matanzas, C.P. 44740, Cuba
Center for Evaluation and Biological Research, Institute of Pharmacy, Havana University, San Lazaro y L, Ciudad de La Habana, Cuba
Polymer Materials Research Group, Department of Organic Chemistry, University of Gent, Krijgslaan 281, S-4, B-9000 Gent. Belgium; reynaldo.villalonga{at}umcc.cu Superoxide dismutase (SOD) was chemically modified with carboxymethylcellulose through two different synthetic procedures: Reductive alkylation with the periodate-oxidized polymer (SOD-CMCox), and the formation of amide linkages through a carbodiimide catalyzed reaction (SODCMCedac). The SOD-CMCox and SOD-CMCedac conjugates contained about 1.81.2mol of polymer per mol of protein, and retained 6878% of the initial catalytic activity, respectively. The glycosidated enzymes were more resistant to inactivation with H2O2 and their plasma half-life times were prolonged to 34.7h 6.6h when compared with 4.8min for native SOD. The anti-inflammatory activity of the enzyme was 22.4 times increased after conjugation with the polymer.
Key Words: superoxide dismutase carboxymethylcellulose anti-inflammatory modified enzyme pharmacokinetics
Journal of Bioactive and Compatible Polymers, Vol. 20, No. 6,
557-570 (2005) |
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