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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III
Keigo Hisamatsu1, Hideaki Unno, Shuichiro Goda
1Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki, Japan.
Bioscience, Biotechnology, and Biochemistry
|May 8, 2009
Abstract:
CEL-III is a hemolytic lectin isolated from Cucumaria echinata. Although recombinant CEL-III (rCEL-III) expressed in Escherichia coli showed very weak hemolytic activity compared with native protein, it was considerably enhanced by refolding in the presence of Ca(2+). This suggests that Ca(2+) supported correct folding of the carbohydrate-binding domains of rCEL-III, leading to effective binding to the cell surface and subsequent self-oligomerization.
