Purification and cell attachment activity of a D-galactose-binding lectin from the skin of sea hare, Aplysia kurodai.
A D-galactose-binding lectin which does not require Ca2+ or reducing reagents to induce activity was purified from skin of sea hare, Aplysia kurodai, by affinity chromatography. Skin lectin was confirmed to be a disulfide-bonded heteromultimer with molecular mass of 200 kDa, consisting of 28 kDa and 26 kDa subunits by SDS-PAGE and two-dimensional SDS-PAGE. Human rhabdomyosarcoma cells attached to and spread on plastic plates coated with lectin. Cell adhesion induced by lectin was completely inhibited by the addition of lactose.
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Department of System Element, Faculty of Science, Yokohama City University, Yokohama, Japan.
D000818:Animals; D001048:Aplysia / Q000737:chemistry*; D002448:Cell Adhesion; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005690:Galactose / Q000378:metabolism; D037161:Galectins; D006384:Hemagglutination; D006388:Hemagglutinins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D008970:Molecular Weight; D014407:Tumor Cells, Cultured
D037161:Galectins; D006388:Hemagglutinins; D005690:Galactose