Total salt-soluble protein was extracted from chickpea Cotyledens and was precipitated with different concentrations of ammonium sulphate into fractions. 0.60% and 60-100%. Albumin was removed from fraction 60-100 by dialysis at 3-5oC against H2O. pH 4.1, and globulin of the fraction was chromatographed on DEAE-cellulose column for separation of vicilin from protein complex. Isolated Vicilin was tested for freedom from contaminants, Chromatoelectrophoretically it was pure. Sedimentation curve also witnessed about its homogeneity. Maximum elution on celite column was with 76% ammonium sulphate concentration. Elution constants on hydroxylapatite and DEAE-cellulose colums were 0.40 M and 0.26 u phosphate buffers respectively. Sedimentation coefficient was 6.72 S. Vicilin was found rich in the isoleucime and poor in arginime in comparison with the results obtained by Boulter and Derbyshire (1971) for the amino acid composition of vicilin of chickpea seed.