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Purification and characterization of four Ca(2+)-dependent lectins from the marine invertebrate, Cucumaria echinata.
Four Ca(2+)-dependent, N-acetylgalactosamine/galactose-specific lectins were purified from the marine invertebrate, Cucumaria echinata (Holothuroidea), by column chromatography on lactosyl-SepharoseExpand
L-ornithine decarboxylase from Hafnia alvei has a novel L-ornithine oxidase activity.
Results suggested that OOD and ODC are identical and that the former is a side reaction of the latter in the presence of O2. Expand
Preparation and Properties of Gelatin-Immobilized β-Glucosidase from Pyrococcus furiosus
Gelatin-immobilized β-glucosidase from Pyrococcus furiosus was enclosed in gelatin gel by cross-linking with transglutaminase and was considerably more thermostable than the native enzyme. Expand
Temperature- and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines.
The cytotoxicity of CEL-III, one of four Ca2+-dependent galactose/N-acetylgalactosamine (GalNAc)-binding lectins from the marine invertebrate Cucumaria echinata, is suggested to be through damaging the plasma membrane by pore-formation in a temperature- and pH-dependent manner. Expand
Carbohydrate-binding properties of the hemolytic lectin CEL-III from the holothuroidea Cucumaria echinata as analyzed using carbohydrate-coated microplate.
The results suggested that the carbohydrate-binding properties of CEL-III are closely related to its hemolytic activity, although an additional interaction between the protein and the lipid bilayer, which is enhanced in the alkaline pH region, also seems to be necessary for its Hemolytic action. Expand
Enantioselective reduction of γ-hydroperoxy-α,β-unsaturated carbonyl compounds catalyzed by lipid-coated peroxidase in organic solvents
Abstract The reduction of racemic γ-hydroperoxy-α,β-unsaturated carbonyl compounds in the presence of lipid-coated horseradish peroxidase as a homogenious catalyst in organic solvents such asExpand