Abstract
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.
