| Literature DB >> 2582021 |
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.Entities:
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Year: 1985 PMID： 2582021 DOI： 10.1016/0165-022x(85)90066-1
Source DB: PubMed Journal: J Biochem Biophys Methods ISSN： 0165-022X