Boletus fulvus lectin (BFL) was isolated from Boletus fulvus, by extraction, ion exchange chromatography on CM Sepharose and DEAE Sepharose followed by gel filtration on Sephacryl S 100. BFL is a homodimer with apparent molecular mass of 32 kDa and composed of two 15.8 kDa subunits that are held together by noncovalent interactions. BFL could agglutinate rabbit erythrocyte, and it exhibited strong hemagglutination activity to rabbit erythrocytes at the concentration 3.9 μg/mL. The result of carbohydrate inhibition assay showed that the gastric mucin, thyroglobulin, ovomucoid and ovalbumin could inhibit the agglutinating activity of BFL. The hemagglutination activity of BFL was stable under 70℃ and in a pH range of 6.0~9.8, while it was weak when temperature was higher than 90℃ and in extreme pH range. Effects of different concentrations of urea and GuHCl on the hemagglutination activity of BFL indicated the increase of denaturant concentration could destroy the structure of BFL gradually.
