4-Nitrophenyl-alpha-D-glucopyranoside, 99%

Chromogenic substrate for alpha-D-glucosidase yielding a yellow solution upon cleavage. Also used for the detection of glucansucrases and for yeast alpha-D-glucosidase and for studies of the crystal structure of the complexes of concanavalin A. 1. Binder T.P., Robyt J.F., p-Nitrophenyl-alpha-D-glucopyranoside, a new substrate for glucansucrases. Carbohydr. Res. 1983, 124, 287-99. 2. Kanellopoulos P.N., Pavlou K., Perrakis A., Agianian B., Vorgias C.E., Mavrommatis C., Soufi M., Tucker P.A., Hamodrakas S.J., The crystal structure of the complexes of concanavalin A with 4'-nitrophenyl-alpha-D-mannopyranoside and 4'-nitrophenyl-alpha-D-glucopyranoside. J. Struct. Biol. 1996, 116, 345-55. 3. Mizuno K., Tachiki T., Extracellular dextran-induced p-nitrophenyl-alpha-D-glucoside-hydrolyzing enzyme of Bacillus circulans KA-304: a producer of Schizophyllum commune-lytic enzyme. Biosci. Biotechnol. Biochem. 1998, 62, 393-5. 4. Muytjens H.L., van der Ros-van de Repe J., van Druten H.A., Free in PMC Enzymatic profiles of Enterobacter sakazakii and related species with special reference to the alpha-glucosidase reaction and reproducibility of the test system. J Clin Microbiol. 1984, 20, 684-6. 5. Oliveira D.E., Santos Neto A.L., Panek A.D., Permeabilization of yeast for in situ determination of alpha-glucosidase. Anal. Biochem. 1981, 113, 188-92. 6. Schram A.W., Brouwer-Kelder B., Donker-Koopman W.E., Loonen C., Hamers M.N., Tager J.M., Use of immobilized antibodies in investigating acid alpha-glucosidase in urine in relation to Pompe's disease. Biochim. Biophys. Acta. 1979, 567, 370-83. 7. Wimmer B., Lottspeich F., Ritter J., Bronnenmeier K., A novel type of thermostable alpha-D-glucosidase from Thermoanaerobacter thermohydrosulfuricus exhibiting maltodextrinohydrolase activity. Biochem. J. 1997, 328, 581-6.