Deactivation of bilirubin oxidase by a product of the reaction of urate and O2
โ Scribed by Chan Kang; Hyosul Shin; Yongchao Zhang; Adam Heller
- Publisher
- Elsevier Science
- Year
- 2004
- Tongue
- English
- Weight
- 287 KB
- Volume
- 65
- Category
- Article
- ISSN
- 1567-5394
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๐ SIMILAR VOLUMES
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NO, was photolyzed with 2288 A radiation at 300" and 423'K in the presence of H 2 0 , The photolysis produces O(lD) atoms which react with CO, and in some cases excess He. H20 to give H O radicals (3) O(lD) + H20 -+ 2 H 0 or are deactivated by CO to O ( 3 P ) atoms (5) O ~D ) The ratio kJkS is temp
Urate oxidase from Candida utilis, an enzyme containing an essential thiol, was examined for its sensitivity to lactoperoxidase, an oxidant present in breast milk. Upon exposure to a system composed of lactoperoxidase, hydrogen peroxide and bromide at moderately alkaline pH, the urate oxidase exhibi