Tomonao Nagao

We don’t have enough information about this author to calculate their statistics. If you think this is an error let us know.
Learn More
The hemolytic lectin CEL-III forms transmembrane pores in the membranes of target cells. A study on the effect of site-directed mutation at Lys405 in domain 3 of CEL-III indicated that replacements of this residue by relatively smaller residues lead to a marked increase in hemolytic activity, suggesting that moderately destabilizing domain 3 facilitates(More)
Introduction CEL-III is a Ca-dependent, Gal/GalNAc-specific lectin purified from sea cucumber Cucumaria echinata, which shows haemolytic activity, especially toward human and rabbit erythrocytes [1]. Hemolysis is caused by the colloid osmotic rupture of the erythrocyte membrane due to the formation of ion-permeable pores by CEL-III oligomer after it has(More)
CEL-III is a Ca(2+)-dependent haemolytic lectin isolated from the marine invertebrate Cucumaria echinata. This lectin binds to Gal/GalNAc-containing carbohydrate chains on the cell surface and, after conformational changes, oligomerizes to form ion-permeable pores in cell membranes. CEL-III also forms soluble oligomers similar to those formed in cell(More)
An extracellular lipase from Pichia burtonii was purified to homogeneity by a combination of DEAE-Sephadex A-50 ion-exchange chromatography, Sephadex G-100 gel filtration, and isoelectric focusing. The purified enzyme preparation showed a single protein band corresponding to a molecular mass of 51 kDa on sodium dodecyl sulphate/polyacrylamide gel(More)
BACKGROUND CEL-III is a hemolytic lectin isolated from the sea cucumber Cucumaria echinata that shows Ca(2+)-dependent Gal/GalNAc-binding specificity. This lectin is composed of two carbohydrate-recognition domains (domains 1 and 2) and an oligomerization domain (domain 3) that facilitates CEL-III assembly in the target cell membrane to form ion-permeable(More)
  • 1