Total salt-soluble protein extract of lentil seeds was fractionated with differenct concentration intervals of ammonium sulphate. Fractions were separated by chromatography on hy­droxylapatite column. Chromatographic fractions were analysed by electrophoresis on polyacrylamide gel.The seeds contained a highly heterogeneous system of individual proteins. Fraction 0-30 was composed of minor protein components and nucleic acids. Fraction 30-60 was represented by primary and secondary globulins. The fraction which preciptated with ammonium sulphate of above 60% con­centration was dominated by vicilin and legumin. Which were inseparable on hydroxylapatite column and had maximum elution at 0.29 M phosphate buffer.