Limulus polyphemus lectin

Fig. 15.—Human IgA, Glycopeptide871 Showing the Carbohydrate-binding Loci for Various Lectins, [a. Limulus polyphemus b, Triticum vulgaris c, Ricinus communis d, Sophora japonica e, Abrus precatorius f, Cytisus sessilifolius g, Phaseolus vulgaris-, h, Canavalia ensiformis i, Lens culinaris j, Pisum sativus k, Vicia faba-, 1, Bandeiraea simplicifolia II m, Solanum tuberosum and n, Ulex europeus II.]...

The neuraminic acid-binding lectin, limulin, has been isolated from the haemolymph of the horseshoe crab, Limulus polyphemus. The amino-acid sequence of 76 residues of this molecule, including 50 amino-acids from the amino-terminus, has been obtained by sequence analysis of the intact protein and its cyanogen bromide-derived fragments. No obvious sequence homology between the invertebrate lectin and vertebrate immunoglobulins was observed. 

Fluorescence polarization of l,6-diphenyl-l,3,5-hexatriene has been used to demonstrate the interaction between vesicles containing gangliosides and the lectin from Limulus polyphemus. ... 

Brandin, E.R., and T.G. Pistole Polyphemin A Teichoic Acid-Binding Lectin from the Horseshoe Crab, Limulus polyphemus. Biochem. Biophys. Res. Commun. 113, 611 (1983). 

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