Author(s): de Smet MJ, Kingma J, Witholt B
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Abstract The effect of toluene on Escherichia coli has been examined. In the presence of Mg2+, toluene removes very little protein, phospholipid, or lipopolysacharide from E. coli. In the absence of Mg2+, or in the presence of EDTA, toluene removes considerably more cell material, including several specific cytoplasmic proteins such as malate dehydrogenase (EC 126.96.36.199). In contrast, glucose-6-phosphate dehydrogenase (EC 188.8.131.52) and glutamate dehydrogenase (EC 184.108.40.206) are not released at all under the same conditions. Cells treated with toluene in the presence of Mg2+ remain relatively impermeable to pyridne nucleotides, while cells treated with toluene in the presence of EDTA become permeable to these compounds. Freeze-fracture electron microscopy shows that toluene causes considerable damage to the cytoplasmic membrane, while the outer membrane remains relatively intact. These results indicate that the permeability characteristics of toluene-treated cells depend at least partly on the state of the outer membrane after the toluene treatment.
This article was published in Biochim Biophys Acta
and referenced in Journal of Aquaculture Research & Development