Purification of a recombinant polyhistidine-tagged glucosyltransferase using immobilized metal-affinity chromatography (IMAC)

DOI	Resolve DOI: https://doi.org/10.1007/978-1-4939-3393-8_9
Author	Search for: De Costa, Fernanda¹; Search for: Barber, Carla J. S.¹; Search for: Pujara, Pareshkumar T.¹; Search for: Reed, Darwin W.¹; Search for: Covello, Patrick S.¹
Editor	Search for: Arthur Germano, Fett-Neto
Name affiliation	National Research Council of Canada. Aquatic and Crop Resource Development
Format	Text, Article
Journal title	Biotechnology of Plant Secondary Metabolism: Methods and Protocols
Series title	Methods in Molecular Biology; no. 1405
ISSN	1064-3745
ISBN	978-1-4939-3391-4 978-1-4939-3393-8
Pages	91–07
Subject	IMAC; His-tagged protein; Glucosyltransferase; Recombinant; Purification
Abstract	Short peptide tags genetically fused to recombinant proteins have been widely used to facilitate detection or purification without the need to develop specific procedures. In general, an ideal affinity tag would allow the efficient purification of tagged proteins in high yield, without affecting its function. Here, we describe the purification steps to purify a recombinant polyhistidine-tagged glucosyltransferase from Centella asiatica using immobilized metal affinity chromatography.
Publication date	2016-02-04
Publisher	Springer
Language	English
Peer reviewed	Yes
NPARC number	23000699
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Record identifier	5b0c1e70-e25c-4cb5-9cc9-1a18db65e5e5
Record created	2016-08-25
Record modified	2020-03-16