Effects of Ca2+on Refolding of the Recombinant Hemolytic Lectin CEL-III
Author(s) -
Keigo Hisamatsu,
Hideaki Unno,
Shuichiro Goda,
Tomomitsu Hatakeyama
Publication year - 2009
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.80793
Subject(s) - recombinant dna , lectin , escherichia coli , chemistry , folding (dsp implementation) , biochemistry , protein folding , microbiology and biotechnology , biology , gene , electrical engineering , engineering
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.
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