Inactivation of Some Thiol-Enzymes by Trichothecene Mycotoxins from Fusarium Species
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概要
- 論文の詳細を見る
Fusarenon-X, neosolaniol and T-2 toxin, 12,13-epoxytrichothecene mycotoxins of Fusarium spp. cause in vitro an inactivation of SH-enzymes such as creatine phosphokinase, lactate dehydrogenase and alcohol dehydrogenase when the enzyme molecules were preincubated with the mycotoxins in the absence of substrates, and the supplement of dithiothreitol prevents this inactivation. Gel-filtration of a mixture containing alcohol dehydrogenase and ^3H-labelled fusarenon-X revealed the formation of a complex [^3H-fusarenon-X-alcohol dehydrogenase] with a molecular ratio of 4 : 1,and dithiothreitol prevented the complex formation. These results indicate that the epoxytrichothecenes bind with the thiol residues of SH-enzyme protein.
- 社団法人日本薬学会の論文
- 1975-10-25
著者
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上野 芳夫
Research Institute For Biosciences Science University Of Tokyo:department Of Toxicology And Microbia
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上野 芳夫
Laboratory of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Tokyo University of Sciences
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松本 洋子
Laboratory of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Tokyo University of Sciences
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松本 洋子
Laboratory Of Microbial Chemistry Faculty Of Pharmaceutical Sciences Tokyo University Of Sciences
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Ueno Yoshio
Research Institute For Biosciences Science University Of Tokyo
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