{"title":"黄嘌呤氧化酶高亲和铁结合","authors":"Glenn F. Vile, Christine C. Winterbourn","doi":"10.1016/S0748-5514(86)80041-1","DOIUrl":null,"url":null,"abstract":"<div><p>Equilibrium dialysis studies on competitive binding of <sup>59</sup>FeCl<sub>3</sub> to xanthine oxidase and citrate or ATP have been carried out. Iron binding to the enzyme was observed in the presence of 0.1 mM of either chelator, suggesting that xanthine oxidase is likely to have iron bound in many in vitro experimental systems and raising the possibility that it may be able to compete for intracellular chelatable iron. One high-affinity-binding site per monomer was found, with an affinity constant of 5 × 10<sup>12</sup> M<sup>−1</sup>. The significance of this iron as a Fenton reaction catalyst is discussed.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 5","pages":"Pages 393-396"},"PeriodicalIF":0.0000,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0748-5514(86)80041-1","citationCount":"5","resultStr":"{\"title\":\"High-affinity iron binding by xanthine oxidase\",\"authors\":\"Glenn F. Vile, Christine C. Winterbourn\",\"doi\":\"10.1016/S0748-5514(86)80041-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Equilibrium dialysis studies on competitive binding of <sup>59</sup>FeCl<sub>3</sub> to xanthine oxidase and citrate or ATP have been carried out. Iron binding to the enzyme was observed in the presence of 0.1 mM of either chelator, suggesting that xanthine oxidase is likely to have iron bound in many in vitro experimental systems and raising the possibility that it may be able to compete for intracellular chelatable iron. One high-affinity-binding site per monomer was found, with an affinity constant of 5 × 10<sup>12</sup> M<sup>−1</sup>. The significance of this iron as a Fenton reaction catalyst is discussed.</p></div>\",\"PeriodicalId\":77737,\"journal\":{\"name\":\"Journal of free radicals in biology & medicine\",\"volume\":\"2 5\",\"pages\":\"Pages 393-396\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1986-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0748-5514(86)80041-1\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of free radicals in biology & medicine\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0748551486800411\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of free radicals in biology & medicine","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0748551486800411","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Equilibrium dialysis studies on competitive binding of 59FeCl3 to xanthine oxidase and citrate or ATP have been carried out. Iron binding to the enzyme was observed in the presence of 0.1 mM of either chelator, suggesting that xanthine oxidase is likely to have iron bound in many in vitro experimental systems and raising the possibility that it may be able to compete for intracellular chelatable iron. One high-affinity-binding site per monomer was found, with an affinity constant of 5 × 1012 M−1. The significance of this iron as a Fenton reaction catalyst is discussed.