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http://hdl.handle.net/20.500.12323/4752Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Seidel, Antonia | - |
| dc.contributor.author | Turner, Rufus | - |
| dc.contributor.author | Dickerhof, Nina | - |
| dc.contributor.author | Khalilova, Irada S. | - |
| dc.contributor.author | Wilbanks, Sigurd M. | - |
| dc.contributor.author | Kettle, Anthony J. | - |
| dc.contributor.author | Jameson, Guy N. L. | - |
| dc.contributor.author | Parker, Heather | - |
| dc.date.accessioned | 2020-09-18T07:38:20Z | - |
| dc.date.available | 2020-09-18T07:38:20Z | - |
| dc.date.issued | 2014-08 | - |
| dc.identifier.citation | Journal of Biological Chemistry | en_US |
| dc.identifier.uri | http://hdl.handle.net/20.500.12323/4752 | - |
| dc.description.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. | en_US |
| dc.language.iso | en | en_US |
| dc.publisher | American Society for Biochemistry and Molecular Biology | en_US |
| dc.relation.ispartofseries | Vol. 289;№ 32 | - |
| dc.title | Uric acid and thiocyanate as competing substrates of lactoperoxidase | en_US |
| dc.type | Article | en_US |
| Appears in Collections: | Publications | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Uric acid and thiocyanate as competing substrates of lactoperoxidase.pdf | 1.86 MB | Adobe PDF | View/Open |
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