猪肺血管紧张素转换酶的提纯  

Purification of angiotensin-converting enzyme in hog lung

作　　者：耿秀芳[1] 李耀辉[2] 李桂芝[1] 孙风祥[1] 王守训[1] 任维栋[1] 

机构地区：[1]潍坊医学院生物化学教研室,山东潍坊261042 [2]潍坊医学院化学教研室,山东潍坊261042

出　　处：《医学研究生学报》2001年第5期428-431,共4页Journal of Medical Postgraduates

摘　　要：目的：探讨纯化猪肺血管紧张素转换酶(ACE)的一个简便方法. 方法：将新鲜猪肺匀浆,上清液通过(NH4)2SO4分级沉淀,Sephadex G-200凝胶过滤,DEAE-Sephacel以及羟基磷灰石柱层析. 结果：由251 g猪肺制备出8.18 mg酶蛋白,活力回收为33%,比活力936.43 U/mg蛋白,较上清液提纯233倍.聚丙烯酰胺凝胶电泳(pH 8.5)显示一条带.SDS-聚丙烯酰胺凝胶电泳测知,相对分子质量为190 000. 结论：该法简便,活力回收高,比活力显著高于同类研究报道的15.6 U/mg蛋白.： Objectives：An improvement method of purification of angiotensin-converting enzyme from hog lung was reported in this paper. Methods:Fresh hog lung was homogenized.The supernatant solution was pre cipitated gradually with 1.62.6 mol/L (NH4)2SO4.It was followed by filtra tion on Sephadex G-200 column,ion exchange chromatography on DEAE-Sephacel column and absorption chromatography on hydroxyapatite column. Resul ts:8.18 mg enzyme protein was obtainted from 251 g hog lung. The recovery of activity was 33.40% with specific activity of 936.4 U/mg protein.ACE was purified 233 folds in comparison with the original supernatant of hog lung. Final enzyme preparation on analytical polyacrylamide gel electro phoresis(pH 8.5) showed one major protein band.The molecular weight was estimated to be approximately 190 000 dalton by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Conclusions：The method is easy,recovery of activity is high and specific activity is greater th an similar reports of 15.6U/mg protein obviously.

关 键 词：血管紧张素转换酶 提纯 肺 猪 肽酰二肽酶 

分 类 号：Q556.3[生物学—生物化学]