{"title":"甲状腺“DT脱氢酶”","authors":"L.J. DeGroot, Ronald Dechene, J. Thompson","doi":"10.1016/0926-6569(64)90181-6","DOIUrl":null,"url":null,"abstract":"<div><p>The enzyme “DT diaphorase”, which mediates transfer of electrons from TPNH or DPNH to dichlorophenol-indophenol is abundant in the thyroid. In common with the enzyme described by Ernster and coworkers<sup>1</sup> in liver, the enzyme is largely present in the soluble portion of the cell, and is inhibited by bishydroxycoumarin, but not by antimycin A. Addition of FAD markedly augments activity.</p><p>The enzyme appears to play little role in oxidative metabolism and could not be related to iodination of tyrosine by thyroid cell particles or a soluble iodinating enzyme derived from the particles.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 223-232"},"PeriodicalIF":0.0000,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90181-6","citationCount":"2","resultStr":"{\"title\":\"Thyroid “DT diaphorase”\",\"authors\":\"L.J. DeGroot, Ronald Dechene, J. Thompson\",\"doi\":\"10.1016/0926-6569(64)90181-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The enzyme “DT diaphorase”, which mediates transfer of electrons from TPNH or DPNH to dichlorophenol-indophenol is abundant in the thyroid. In common with the enzyme described by Ernster and coworkers<sup>1</sup> in liver, the enzyme is largely present in the soluble portion of the cell, and is inhibited by bishydroxycoumarin, but not by antimycin A. Addition of FAD markedly augments activity.</p><p>The enzyme appears to play little role in oxidative metabolism and could not be related to iodination of tyrosine by thyroid cell particles or a soluble iodinating enzyme derived from the particles.</p></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 2\",\"pages\":\"Pages 223-232\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-11-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90181-6\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926656964901816\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964901816","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The enzyme “DT diaphorase”, which mediates transfer of electrons from TPNH or DPNH to dichlorophenol-indophenol is abundant in the thyroid. In common with the enzyme described by Ernster and coworkers1 in liver, the enzyme is largely present in the soluble portion of the cell, and is inhibited by bishydroxycoumarin, but not by antimycin A. Addition of FAD markedly augments activity.
The enzyme appears to play little role in oxidative metabolism and could not be related to iodination of tyrosine by thyroid cell particles or a soluble iodinating enzyme derived from the particles.
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