期刊
BIOTECHNOLOGY AND BIOENGINEERING
卷 74, 期 2, 页码 164-171出版社
JOHN WILEY & SONS INC
DOI: 10.1002/bit.1106
关键词
C-LYTA; affinity tag; heterologous expression; yeast
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. (C) 2001 John Wiley & Sons, Inc.
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