Sephadexg-25 column chromatography was used to separate hydrolyzed sheep bone collagen prepared with neutral protease to molecules of larger than 5000 D in size and two ACE inhibitory peptides, peaks 1 and 2, both of which had an average inhibitory rate of over 92%. MALDI-TOF-MS （matrix assisted laser desorption ionization/time of flight MS） analysis showed that both peaks consisted of more than 30 fragments and the peptide showing the highest intensity was 1077.36 D in peak 1 and 1048.47D in peak 2. The total amino acid content of peak 1 was 23.49 g/100 g and of peak 28.32 g/100 g. Eight essential amino acids were found in both of them, and three nonessential amino acids such as Gly, Pro and Ghi were also abundantly contained.%利用中性蛋白酶酶解羊骨得到羊骨胶原降血压肽粗品的基础上，研究SephadexG－25凝胶过滤层析方法埘羊骨胶原降血压肽粗品的分离纯化效果。结果显示：SephadexG－25凝胶过滤层析将分子质量大于5000D的大分r滤去，得到了峰1和峰2两种多肽产品，其血管紧张素转化酶（ACE）抑制率均达到92％以上。采用1毛行质谱对峰1和峰2多肽产品的分f质量进行质谱测定，肽质量指纹图谱显示，利用SephadexG－25凝胶过滤麒析订浊，并不能得到羊骨胶原降血压肽纯品，峰1和峰2均由多组分组成，分别出现30多个片段，其
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