![Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5925/TOC-Subject-Sample-2021-Bioscience.jpg"})
Abstract
Antioxidant enzymes superoxide dismutase (SOD) and catalase were cross-linked with each other to form an antioxidant complex (polySOD-catalase). SOD activity was unaffected after polymerization reaction initiated by glutaraldehyde, and catalase activity was modestly decreased. In an oxidative stress model, where a xanthine/xanthine oxidase system was employed to generate superoxide radicals, catalase located at sufficient proximity to SOD after polymerization reaction provided effective protection for SOD from oxidative damage. In vivo evaluation indicated the antioxidant complex of polySOD-catalase had an extended circulation time suitable for therapeutic utility. As measured in anesthetized rate, polySOD-catalase can remain circulating with a half-life of as much as 6 h. Such a polymerization formulation could be a candidate therapeutic agent for age-related diseases associated with reactive oxygen species.
Declaration of interest: This work was supported by Science and Technology Research Fund no. B03-01 from the University of Jinan. The authors alone are responsible for the content and writing of the paper.