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https://hdl.handle.net/1959.11/5969
Title: | Purification and properties of a glutathione peroxidase from Southern bluefin tuna ('Thunnus maccoyii') liver | Contributor(s): | Thompson, Janene L (author); Thomas, Philip (author); Schuller, Kathryn A (author) | Publication Date: | 2006 | DOI: | 10.1016/j.cbpb.2006.01.011 | Handle Link: | https://hdl.handle.net/1959.11/5969 | Abstract: | A glutathione peroxidase (GPX) protein was purified approximately 1000-fold from Southern bluefin tuna (Thunnus maccoyii) liver to a final specific activity of 256 μmol NADPH oxidised min−¹ mg−¹ protein. Gel filtration chromatography and denaturing protein gel electrophoresis of the purified preparation indicated that the protein has a native molecular mass of 85 kDa and is most likely a homotetramer with subunits of approximately 24 kDa. The Km values of the purified enzyme for hydrogen peroxide, cumene hydroperoxide, t-butyl hydroperoxide and glutathione were 12, 90, 90 and 5900 μM, respectively. The Km values for cumene hydroperoxide and t-butyl hydroperoxide were approximately 8-fold greater than the Km value for hydrogen peroxide. Thus, the SBT liver GPX has a considerably greater affinity for hydrogen peroxide than for the other two substrates. The pH optimum of the purified enzyme was pH 8.0. Immunoblotting experiments with polyclonal antibodies, raised against a recombinant human GPX, provided further evidence that the purified SBT enzyme is a genuine GPX. | Publication Type: | Journal Article | Source of Publication: | Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology, 144(1), p. 86-93 | Publisher: | Elsevier Inc | Place of Publication: | United States of America | ISSN: | 1878-1659 1532-0456 |
Fields of Research (FoR) 2008: | 069999 Biological Sciences not elsewhere classified | Socio-Economic Objective (SEO) 2008: | 839999 Animal Production and Animal Primary Products not elsewhere classified | Peer Reviewed: | Yes | HERDC Category Description: | C1 Refereed Article in a Scholarly Journal |
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Appears in Collections: | Journal Article |
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