## 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
✦ LIBER ✦
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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