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Localization of glycosidases with naphthyl substrates

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Unsubstituted naphthyl substrates were found to be superior to substituted naphthyl, indolyl and hydroxyquinoline substrates for the histochemical demonstration of α-mannosidase, α-galactosidase, hetero-β-glycosidase, glucoamylase and sucrase-isomaltase, equivalent for β-N-acetylglucosaminidase and lactase-β-glucosidase, and inferior for β-glucuronidase and acid β-galactosidase. Aldehyde fixation is necessary for the localization of lysosomal glycosidases with naphthyl substrates.i-naphthyl substrates are suitable for the detection of acid glycosidases in lysosomes and hetero-β-glycosidase in the cytoplasm of animal cells, and 2-naphthyl substrates can be employed for the demonstration of microvillous glycosidases and for the evaluation of the total activity of soluble glycosidases with semipermeable membranes. When naphthyl substrates are used coupling should be carried out simultaneously and hexazotized pararosaniline is the coupling reagent of choice.

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  1. Department of Anatomy, University of Würzburg, Würzburg, Germany

    R. Gossrau

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Gossrau, R. Localization of glycosidases with naphthyl substrates. Histochem J 8, 271–282 (1976). https://doi.org/10.1007/BF01003816

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