Protein purification with C-terminal fusion of maltose binding protein.

Abstract:

:For affinity-chromatography-based purification of proteins that are prone to abnormal termination of translation or that may not be modified at their N-termini, affinity tags are needed which can be fused to the C-terminus. In this publication we describe that maltose binding protein (MBP) fused to the C-terminus of the plant photoreceptor phytochrome B allows purification of the fusion protein via amylose affinity chromatography. After overexpression in yeast a 125-fold enrichment could be achieved. The spectral properties of phytochrome B were not impaired by the fusion and purification. These results demonstrate that not only the widely used N-terminal fusions of MBP but also C-terminal fusions can be employed for protein purification.

journal_name

Protein Expr Purif

authors

Hennig L,Schäfer E

doi

10.1006/prep.1998.0969

subject

Has Abstract

pub_date

1998-12-01 00:00:00

pages

367-70

issue

3

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(98)90969-X

journal_volume

14

pub_type

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