Affinity chromatography of mustard beta-amylase on starch columns.
J Biochem Biophys Methods
; 10(5-6): 315-20, 1985 Mar.
Article
em En
| MEDLINE
| ID: mdl-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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Plantas
/
Beta-Amilase
/
Amilases
Idioma:
En
Revista:
J Biochem Biophys Methods
Ano de publicação:
1985
Tipo de documento:
Article