title: Effects of detergents on the oligomeric structures of hemolytic lectin CEL-III as determined by small-angle X-ray scattering.
abstract: Hemolytic lectin CEL-III isolated from the sea cucumber Cucumaria echinata forms transmembrane pores by self-oligomerization in target cell membranes. It also formed soluble oligomers in aqueous solution upon binding with specific carbohydrates under conditions of high pH and a high salt concentration. The size of the soluble CEL-III oligomers decreased when treated with detergents such as Triton X-100 and SDS. Small-angle X-ray scattering measurements suggested that the dissociated unit of the oligomer was a tightly associated CEL-III heptamer. Without detergents in solution, these heptamers further assembled into larger 21mer oligomers, comprising three heptamers held together by relatively weak hydrophobic interactions.
authors.affiliation: Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Japan.
authors.forename: Shuichiro
authors.initials: S
authors.lastname: Goda
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Sadakata
authors.forename: Hideaki
authors.initials: H
authors.lastname: Unno
authors.forename: Tomomitsu
authors.initials: T
authors.lastname: Hatakeyama
mesh_terms: D003902:Detergents / Q000494:pharmacology*; D006461:Hemolysis; D037102:Lectins / Q000737:chemistry*; D055503:Protein Multimerization / Q000187:drug effects*; D020836:Protein Structure, Quaternary / Q000187:drug effects; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction
chemical_list: C402644:CEL-III lectin, Cucumaria echinata; D003902:Detergents; D037102:Lectins