Affinity chromatography of mustard β-amylase on starch columns

dc.contributor.author	Subbramaiah, K.
dc.contributor.author	Sharma, R.
dc.date.accessioned	2022-03-27T03:49:58Z
dc.date.available	2022-03-27T03:49:58Z
dc.date.issued	1985-01-01
dc.description.abstract	An affinity chromatography method for purification of β-amylase from cytoledons of whit mustard seedlings (Sinapsi alba L.) is described. β-Amylase is bound to starch column, while other contaminating proteins are eluted with the binding buffer. The bound β-amylase is eluted by including dextrin (1%, w/v) in binding buffer. This method yielded a homogenous preparation of β-amylase enzyme, which migrated as a single polypetide band in SDS electrophoresis. © 1985.
dc.identifier.citation	Journal of Biochemical and Biophysical Methods. v.10(5-6)
dc.identifier.issn	0165022X
dc.identifier.uri	10.1016/0165-022X(85)90066-1
dc.identifier.uri	https://www.sciencedirect.com/science/article/abs/pii/0165022X85900661
dc.identifier.uri	https://dspace.uohyd.ac.in/handle/1/5683
dc.subject	affinity chromatography
dc.subject	starch column
dc.subject	β-amylase
dc.title	Affinity chromatography of mustard β-amylase on starch columns
dc.type	Journal. Article
dspace.entity.type

Now showing 1 - 1 of 1