title: Affinity chromatography of mustard beta-amylase on starch columns.
abstract: An affinity chromatography method for purification of beta-amylase from cotyledons of white mustard seedlings (Sinapis alba L.) is described. beta-Amylase is bound to starch column, while other contaminating proteins are eluted with the binding buffer. The bound beta-amylase is eluted by including dextrin (1%, w/v) in binding buffer. This method yielded a homogeneous preparation of beta-amylase enzyme, which migrated as a single polypeptide band in SDS gel electrophoresis.
authors.forename: K
authors.initials: K
authors.lastname: Subbaramaiah
authors.forename: R
authors.initials: R
authors.lastname: Sharma
mesh_terms: D000681:Amylases / Q000032:analysis*; D002846:Chromatography, Affinity / Q000379:methods; D010944:Plants / Q000032:analysis*; D013213:Starch; D001614:beta-Amylase / Q000032:analysis*
chemical_list: D013213:Starch; D000681:Amylases; D001614:beta-Amylase