Choline‐binding domain as a novel affinity tag for purification of fusion proteins produced in Pichia pastoris
Biotechnology and Bioengineering2001Vol. 74(2), pp. 164–171
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Julio Caubín, Humberto Martı́n, Alejandra A. Roa, Inmaculada C. Cosano, Mercedes Pozuelo, J. M. de la Fuente, José-María Sánchez-Puelles, Marı́a Molina, César Nombela
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 based on the fusion of C-LYTA to the protein of interest. We show that C-LYTA can be efficiently expressed and secreted in this host. Tagged proteins fused to this binding domain can be purified on inexpensive DEAE matrices. It therefore provides a useful system for the purification of recombinant proteins with high specificity suitable for industrial purposes.
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