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Attempts to engineer anEscherichia coliDNA-binding protein as a tool for affinity purification of heterologous proteins

✍ Scribed by R. Caswell; A. Lyddiatt; S. Busby; M. Downham


Publisher
Springer-Verlag
Year
1993
Tongue
English
Weight
498 KB
Volume
7
Category
Article
ISSN
0951-208X

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✦ Synopsis


Restriction sites were introduced into the Eschcrichia coli melR gene that facilitated the fusion of other proteins to MelR. Both R-galactosidase and the constant domain of the human IgG kappa light chain were fused to MelR. However, whilst unmodified MelR could be over-expressed, neither MelR fusion protein was over-produced. Addition of an extra domain to MelR leads to reduced expression in a number of genetic backgrounds.


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Choline-binding domain as a novel affini
✍ J. Caubín; H. Martín; A. Roa; I. Cosano; M. Pozuelo; J. M. de la Fuente; J. M. S 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 511 KB

## Abstract The choline‐binding domain (ChoBD) of the carboxy‐terminal region of the __Streptococcus pneumoniae__ amidase LYTA (C‐LYTA) presents a strong affinity for tertiary amines. We report a method for single‐step purification of proteins expressed in the methylotrophic yeast __Pichia pastoris