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Title: Uric acid and thiocyanate as competing substrates of lactoperoxidase
Authors: Seidel, Antonia
Turner, Rufus
Dickerhof, Nina
Khalilova, Irada S.
Wilbanks, Sigurd M.
Kettle, Anthony J.
Jameson, Guy N. L.
Parker, Heather
Issue Date: Aug-2014
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Journal of Biological Chemistry
Series/Report no.: Vol. 289;№ 32
Abstract: The physiological function of urate is poorly understood. It may act as a danger signal, an antioxidant, or a substrate for heme peroxidases. Whether it reacts sufficiently rapidly with lactoperoxidase (LPO) to act as a physiological substrate remains unknown. LPO is a mammalian peroxidase that plays a key role in the innate immune defense by oxidizing thiocyanate to the bactericidal and fungicidal agent hypothiocyanite. We now demonstrate that urate is a good substrate for bovine LPO.
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