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  • Title: Choline-binding domain as a novel affinity tag for purification of fusion proteins produced in Pichia pastoris.
    Author: Caubín J, Martín H, Roa A, Cosano I, Pozuelo M, de La Fuente JM, Sánchez-Puelles JM, Molina M, Nombela C.
    Journal: Biotechnol Bioeng; 2001 Jul 20; 74(2):164-71. PubMed ID: 11370005.
    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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