摘要
目的从猪骨胶原蛋白酶解物中分离出高纯度的血管紧张素转换酶抑制剂。方法将胶原蛋白酶解物用双蒸水溶解 ,先上SephadexG 2 5柱 ,用含有 10mmol/L吡啶的 0 .6mol/L醋酸溶液洗脱 ,收集对血管紧张素转换酶有抑制作用的峰值部分冻干 ;再上血管紧张素转换酶抑制剂亲和柱洗脱 ,测定各收集管洗脱液的比抑制活力 ,收集峰值部分冻干。结果亲和色谱柱洗脱液峰值管比抑制活力达 14 5 0u/mg,为粗提液的 90 6倍 ,活力回收率为 12 .1%。结论利用亲和色谱法 ,能够从猪骨胶原蛋白酶解物中分离出高纯度的血管紧张素转换酶抑制剂。
PurposeTo isolate and to purify angiotensin converting enzyme inhibitor (ACEI) from pig bone collagenase hydrolysate. MethodsThe hydrolysate was dissolved in double distilled water and chromatographied on Sephadex G-25 column eluted with 0.6 mol/L acetic acid containing 10 mmol/L pyridine. The active fraction was freezing-dried and further purified with an ACEI affinity column.ResultsThe specific inhibition activity of elution peak of ACEI affinity column was up to 1 450 U/mg, and the recovery rate of activity was 12.1%. The purity of eluent was 906 times higher than that of the crude extract.ConclusionThe high purity ACEI was isolated from pig bone collagenase hydrolysate using affinity chromatography.
出处
《中国生化药物杂志》
CAS
CSCD
2004年第6期347-349,共3页
Chinese Journal of Biochemical Pharmaceutics
关键词
亲和色谱
胶原蛋白
酶解物
纯化
血管紧张素转换酶抑制剂
affinity chromatography
collagenase hydrolysate
purification
angiotensin converting enzyme inhibitor
