Common or cultivated garlic (Allium sativum) is a species of monocotyledonous perennial vegetable plant whose bulbs, with a strong smell and taste, are often used as a condiment in cooking.

Allium sativum lectin (ASA) is isolated from the garlic bulbs and purified by affinity chromatography followed by gel filtration. It is a dimer of two subunits with a molecular weight of 24,000 with an isoelectric point between pH 7.2 and pH 7.4. 

The sugar specificities of this lectin can be elucidated by hemagglutination inhibition and a coupled enzyme assay. The hemagglutination inhibition study confirms the specificity of this lectin for D-mannose, while a sensitive enzyme assay allows detailed binding specificities to be examined. The ASA binding sites contain a number of mannose residues, with a sugar eluted from the mannose. Interaction with glycoproteins suggests that lectin not only recognizes internal mannose, but also binds to the central pentasaccharide of nitrogen-bound glycans, even when sialylated. Although the binding site may be resistant to terminal sialic acids and residues of the penultimate galactose, the removal of sialic acids increases potency.