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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Ultracytochemical localization of aldehyde dehydrogenase in Acinetobacter calcoaceticus.

A membrane-bound aldehyde dehydrogenase is induced in Acinetobacter calcoaceticus grown on aliphatic hydrocarbons as sole carbon source. This enzyme is NADP-dependent and is able to oxidize medium- and long-chain aliphatic aldehydes to their corresponding fatty acids. Electron micrographs of sectioned alkane-adapted bacteria showed hydrocarbon inclusions in the cytoplasmic matrix. The cytochemical phenazine methosulphate-tetranitro tetrazolium blue capture reaction allowed to localize the activity of the aldehyde dehydrogenase near the surface of these inclusions. At the same location we also found a NADPH tetrazolium-reducing activity.[1]

References

  1. Ultracytochemical localization of aldehyde dehydrogenase in Acinetobacter calcoaceticus. Sorger, H., Aurich, H., Fricke, B., Vorisek, J. J. Basic Microbiol. (1986) [Pubmed]
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