A lectin detected in haemolymph from the Australian spiny lobster Panulirus cygnus agglutinated human ABO Group A cells to a\r\nhigher titre than Group O or B. The lectin also agglutinated rat and sheep erythrocytes, with reactivity with rat erythrocytes strongly\r\nenhanced by treatment with the proteolytic enzyme papain, an observation consistent with reactivity via a glycolipid. The lectin,\r\npurified by affinity chromatography on fixed rat-erythrocyte stroma, was inhibited equally by N-acetylglucosamine and N-acetylgalactosamine.\r\nComparison of data from gel filtration of haemolymph (behaving as a 1,800,000 Da macromolecule), and polyacrylamide\r\ngel electrophoresis of purified lectin (a single 67,000 Da band), suggested that in haemolymph the lecin was amultimer.\r\nThe purified anti-A lectin autoprecipitated unless the storage solution contained chaotropic inhibitors (125 mmol/L sucrose:\r\n500 mmol/L urea). The properties of this anti-A lectin and other similar lectins are consistent with a role in innate immunity\r\nin these invertebrates.
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