title: Purification of alpha-mannosidase activity from Indian lablab beans.
abstract: Seeds of Dolichos lablab var. typicus (Indian lablab beans) contain a glucose/ mannose specific lectin that was affinity purified on Sepharose mannose columns in our laboratory. The unbound fraction from this matrix showed alpha-mannosidase activity. In the present study this has been purified to homogeneity by a combination of ion-exchange, hydrophobic chromatography and gel filtration. Purified alpha-mannosidase had an apparent molecular weight of 195,000 +/- 5,000 with 4.5% carbohydrate. On SDS-PAGE under reducing conditions, the enzyme dissociated into two major bands corresponding to Mr 66,000 and Mr 44,000. An antibody to the well studied jack bean alpha-mannosidase cross-reacts with the enzyme from the lablab beans suggesting antigenic similarity between these two legume mannosidases.
authors.affiliation: Department of Biochemistry, School of Life Sciences, University of Hyderabad, India.
authors.forename: R B
authors.initials: RB
authors.lastname: Tulasi
authors.forename: S K
authors.initials: SK
authors.lastname: Nadimpalli
mesh_terms: D015153:Blotting, Western; D007887:Fabaceae / Q000201:enzymology*; D008361:Mannosidases / Q000302:isolation & purification* / Q000378:metabolism; D010940:Plant Proteins / Q000302:isolation & purification* / Q000378:metabolism; D010946:Plants, Medicinal; D043323:alpha-Mannosidase
chemical_list: D010940:Plant Proteins; D008361:Mannosidases; D043323:alpha-Mannosidase