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Title: [beta-Glucosidases specific for the cyanogenic glucoside triglochinin from Alocasia macrorrhiza Schott: further characterization of properties (author's transl)]. Author: Hösel W, Klewitz O. Journal: Hoppe Seylers Z Physiol Chem; 1977 Aug; 358(8):959-66. PubMed ID: 411729. Abstract: All beta-glucosidases extracted and separated from a plant of Alocasia macrorrhiza are almost entirely specific for triglochinin. The hexameric beta-glucosidase has been shown to dissociate in dimers without any alteration of activity. Reaggregation could only be demonstrated using bifunctional reagents like glutaraldehyde. Treatments of beta-glucosidase with various chemicals (e. g. glutaraldehyde, dodecyl sulfate) decreased the activity for triglochinin more than the activity for 4-nitrophenyl glucoside. On the other hand, specific reagents like bromocondurite or p-chloromercuribenzoate caused identical inactivations measured with various substrates. It seems possible that the different beta-glucosidases splitting triglochinin arose during purification from the hexameric form which occurs in the plant.[Abstract] [Full Text] [Related] [New Search]