ISSN: 0973-7510

E-ISSN: 2581-690X

Runsong Xiong, Sirajo Umar and Jinchun Chen
1College of Life Science and Technology, Beijing University of Chemical Technology, Beijing – 100 029, P. R. China.
J Pure Appl Microbiol. 2013;7(4):2909-2914
© The Author(s). 2013
Received: 10/03/2013 | Accepted: 21/04/2013 | Published: 30/12/2013
Abstract

Uricase is an important enzyme in purine degradation and receives considerable interests in therapy of hyperuricaemia. But as a heterogeneous protein, it may trigger immunoreactions when applied in human body. To reduce its immunogenicity, we designed three modified uricases, in which bovine lactoferricin was used as molecular modifier and embedded into baboon uricase by recombinant technology. In vitro immunological assay revealed decrease in uricase’s immunogenicity corresponding to the number of modifiers in molecule and the maximum decrease was 48.67%. This study presents the possibility of using small peptide as modifier to reduce the immunogenicity of protein and provides a new clue for molecular modification.

Keywords

Baboon uricase, Bovine lactoferricin, Molecular modification, Immunogenicity

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© The Author(s) 2013. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.