Abstract: The pepsin hydrolysate of porcine hemoglobin as raw material was used for adsorption and desorption through using macroporous resin DA201-C and Sephadex LH-20 chromatogram, then three antihypertensive components were obtained;and to collect and to study on physicochemical properties of ACE inhibitory peptideα-Ⅱthat possessing the largest ACE inhibitory activity.The results showed that:ACE inhibitory peptide of porcine hemoglobin was separaed by macroporous resin DA201-C and the IC₅₀ was 0.87mg/mL;next separaed by Sephadex LH-20 and IC₅₀ was 0.21mg/mL.The lowest solubility of ACE inhibitory peptides of porcine hemoglobin (α-Ⅱ) was 50.37%at pH 7;and this fraction (α-Ⅱ) demonstrated high stability against gastrointestinal proteases, temperature 25～55℃and pH<7.But ACE inhibitory activity could reduce rapidly when the NaCl concentration exceeded 0.6mol/L.