In the present study, an angiotensin seedpods of scarlet runner beans (Phaseolus coccineus) was partially process: acetone precipitation and gel filtration chromatography. The ACE inhibitory activities of all fractions were determined by a spectrophotometric method. The amino acid composition, effect of temperature, pH, digestive enzymes and metal ions on the activity of the partially were determined. From the results, the crude proteins from seedpod specific inhibitoryactivity of 0.064±0.004μmol/min/mg after acetone precipitation. Gel filtration chromatography with sephadex G-50 further increased the specific inhibitory activity purification fold of 3.40 and yield of Glutamic acid at 13.63g/100g protein being highest. The optimum pH and temperature of the peptide was 7.0 and 40 0 C, respecti inhibited by Na + , Mg 2+ , K + , and Ca (p<0.05) decreased the activity of the partially shown that angiotensin-converting enzyme coccineus, but the purification steps needs to be modified to obtain a peptide with higher yield.