CEL-III is a Ca2+-dependent and galactose-specific lectin purified from the sea cucumber, Cucumaria echinata; it exhibits hemolytic and hemagglutinating activities. CEL-III consists of the following three distinct domains: two N-terminal carbohydrate-binding domains (1 and 2), which adopt β-trefoil folds such as the B-chain of ricin and are members of the (QXW)3 motif family, and domain 3, an oligomerization domain. After binding to the cell surface carbohydrate chains through domains 1 and 2, domain 3 self-associates to form transmembrane pores composed of CEL-III heptamers, leading to cell lysis or death. In this chapter, the purification and carbohydrate-coated microplate binding assay of CEL-III are described.
CITATION STYLE
Hatakeyama, T. (2020). Galactose-specific, hemolytic lectin CEL-III from cucumaria echinata. In Methods in Molecular Biology (Vol. 2132, pp. 159–164). Humana Press Inc. https://doi.org/10.1007/978-1-0716-0430-4_16
Mendeley helps you to discover research relevant for your work.