Galactose-binding protein which recognizes specific carbohydrate structures and agglutinates a variety of animal cells by binding to cell-surface glycoproteins and glycolipids. Calcium-dependent lectin. Shows high hemagglutinating activity in the presence of human erythrocytes, which are agglutinated with a minimum hemagglutination concentration (MHC) of 2.5-0.35 ug/ml. Causes indirect nephrotoxicity. Causes reductions in perfusion pressures, renal vascular resistance, urinary flow, glomerular filtration rate, sodium, potassium and chloride tubular transport. Its effects may be caused by the release of inflammatory mediators. Homodimer; disulfide-linked. Expressed by the venom gland. Hemagglutination activity is inhibited by D-lactose (MIC=1.75 mM), D-galactose (MIC=0.75 mM) and D-raphinose (MIC=3.5 mM). Is not inhibited by D-glucose, D-sucrose, D-maltose, D-mannose, D-fructose, D-threalose, and methyl-manopyrosonide (PubMed:15381156). Does not induce direct vasoactive effects in perfused arteriolar mesenteric bed, and does not potentiate bradykinin contraction in the ileum. Belongs to the true venom lectin family. The same name has been given to a lectin from Bothropoides pauloensis (AC P86970).