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Partial purification and biochemical characterization of a soluble alpha-glucosidase from Entamoeba histolytica


Partial purification and biochemical characterization of a soluble alpha-glucosidase from Entamoeba histolytica



FASEB Journal 15(5): A870



ISSN/ISBN: 0892-6638

During synthesis of N-glycans, the glucotriose unit of the lipid-linked intermediate Dol-P-P-GlcNac2Man9Glc3 is removed by the tandem action of processing alpha-glucosidases I and II prior to transfer of the oligosaccharide portion to nascent polypeptides in the lumen of the endoplasmic reticulum. In experiments aimed to the elucidation of the mechanisms of assembly and secretion of glycoproteins in the parasite protozoan E. histolytica, we have identified and characterized enzymes that catalyze essential steps in protein glycosylation. A soluble alpha-glucosidase presumptively related to N-glycoprotein processing was partially purified by a three-step procedure consisting of ion exchange, size exclusion and adsorption chromatographies in Mono Q, Sepharose CL6B and hydroxyapatite columns, respectively. The enzyme was purified 2356-fold over the starting material with a yield of 18% after the last step. Studies with alpha-glucosidase inhibitors such as castanospermine, 1-deoxynojirimycin and australine and determination of linkage specificity using a number of alpha-linked dissaccharides suggest that the enzyme corresponds to a general metabolism glycosidase, probably an isomaltase, apparently not involved in glycoprotein processing.

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Accession: 035463951

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