Seed globulins ofCajanus cajan a widely cultivated legume were purified and characterised. About 78% of the seed proteins were salt soluble, out of which 61% were globulins which were further separated into three fractions. The ∞ fraction was insoluble at pH 4.7 and consisted of two subfractions. Fraction β and γ were soluble at pH 4.7. All the fractions were characterised as glycoproteins by cesium chloride centrifugation. The proteins consisted of subunits which were not held together by covalent disulphide linkages. Amino acid analysis of the different globulin fractions showed that the γ fraction was comparatively rich in sulphur amino acids.