Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III.
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.
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki, Japan.
Keigo
K
Hisamatsu
Hideaki
H
Unno
Shuichiro
S
Goda
Tomomitsu
T
Hatakeyama
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D018360:Crystallography, X-Ray; D006461:Hemolysis / Q000187:drug effects*; D037102:Lectins / Q000737:chemistry* / Q000494:pharmacology*; D008958:Models, Molecular; D011487:Protein Conformation; D020673:Protein Renaturation / Q000187:drug effects*; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry* / Q000494:pharmacology*
C402644:CEL-III lectin, Cucumaria echinata; D037102:Lectins; D011994:Recombinant Proteins; D002118:Calcium