Proteins were isolated from chickpea flour by micellization and isoelectric precipitation techniques. Protein content ranged from 84.8-87.8%. Denaturation temperature and transition enthalpy, by differential scanning calorimetry, were higher for micelle than for isoelectric proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed a molecular weight distribution between 16.6-66.4 kD for micelle and 14.9-84.2 kD for isoelectric proteins. Most functional properties compared favorably to a commercial soy isolate. In general, most essential amino acids of chickpea isolates were at acceptable levels compared to a reference pattern. High values of in vitro digestibility and calculated PER were obtained for the isolates.