Inhibition of glycosidases by aldonolactones of corresponding configuration

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Abstract
Thirteen aldonolactones of the common sugars were tested on the glycosidases of mixed rumen microorganisms, lucerne seed, limpet visceral hump and mouse liver, using as substrates p-nitro-phenyl [alpha]-glucoside, o-nitrophenyl [beta]-glucoside [beta]-galactoside, phenyl [beta]-glucoside, [alpha]-galactoside, [alpha]-mannoside, [beta]-mannoside, -[beta]xyloside, phenophthalein [beta]-ghicuronide. With the exception of [alpha]-galactosidase, the [alpha]- and [beta]-glycosidases were powerfully inhibited by aldonolactones of corresponding structure and configuration. In many instances, the aldonolactones were completely specific in their actions, but in others some cross-effects were noted that could usually be attributed to a lack of complete specificity on the part of an enzyme.