Lotus tetragonolobus lectin (LTL) is isolated from lotus seeds and is composed of 240 amino acid residues. LTL is a glycoprotein with a molecular weight of 107 kDa and consists of four subunits. This lectin has different isoelectric points of pH 7.3, 7.6, 7.9, 8.2 and a carbohydrate specificity toward α-linked L-fucose containing oligosaccharides, it is most inhibited by L-fucose. Although many of the binding properties of Lotus lectin are similar to those of Ulex europaeus lectin I, the binding affinities and some specificities for oligosaccharides are markedly different between these fucose-specific lectins. 

LTL is a fucose-binding anti-H(O) lectin. Reports show that a minimum hemagglutinating dose of 3.3 µg/ml of the purified lectin against neuraminidase-treated human O erythrocytes, 26.4 µg/ml against B erythrocytes, and 105.6 µg/ml against A erythrocytes. Transitional cell carcinoma of the human urinary bladder tend to metastasize when it strongly expresses binding sites for LTL.