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猪肺血管紧张素转换酶的提纯
引用本文:陈兰英,田敏,谢贵福.猪肺血管紧张素转换酶的提纯[J].中国生物化学与分子生物学报,1988,4(4):345-351.
作者姓名:陈兰英  田敏  谢贵福
作者单位:中国医学科学院心血管病研究所 北京 (陈兰英,田敏),中国科学院生物物理研究所 北京(谢贵福)
摘    要:本文报道了猪肺血管紧张素转换酶(ACE)的提纯方法及其鉴定,并讨论了方法的改进。肺匀浆经1.6—2.6mol/L硫酸铵沉淀,Sephadex G-200凝胶过滤,DEAE-Sephaeel及羟基磷灰石柱层析步骤,从168克肺中获得4.5毫克酶蛋白纯品。活力回收45.2%,比活力15.6单位/毫克蛋白;和匀浆上清比较,提纯390倍。经聚丙烯酰胺凝胶电泳(pH8.3)鉴定为一条带。按SDS聚丙烯酰胺凝胶电泳(SDS-PAGE)测得其分子量为132,000道尔顿。酶蛋白在-30℃貯存10月,比活力丢失30%。

关 键 词:血管紧张素转换酶  猪肺  纯化  
收稿时间:1988-08-20

PURIFICATION OF ANGIOTENSIN CONVERTING ENZYME FROM HOG LUNG
Chen,Lan-ying Tian,min.PURIFICATION OF ANGIOTENSIN CONVERTING ENZYME FROM HOG LUNG[J].Chinese Journal of Biochemistry and Molecular Biology,1988,4(4):345-351.
Authors:Chen  Lan-ying Tian  min
Institution:(Cardiovascular Institute,Chinese Academy of Medical Sciences, Beijing)Xie, Gui-fu(Institute of Biophysics, Academia Sinica, Beijing
Abstract:In this paper, the purification and identification of angiotensin converting enyme (ACE) from hog lung were reported and the improvements of the method were also discussed. 4.5 mg of enzyme protein from 168 gm of homogenized hog lung was obtained after purifying the latter with 1.6-2.6 mol/L ammonium sulfate fractionation, gel filtration on Sephadex G-200 column, and ion-exchange chro-matography on DEAE-Sephacel and hydroxylapatite columns. The recovery of activity was 45.2% with specific activity of 15.6 units/nig protein. ACE was purified 390-fold in comparison with the original homogenate supernatant of hog lungs.The final enzyme preparation showed one protein band on polyacrylamide gel electro-phoresis. Its molecular weight is 132,000 dalton by sodium dodecylsulfate (SDS) polyacrylamide gel method.About 30% of its specific activities is lost after storage at -30℃ for ten months.
Keywords:Angiotensin converting enzyme(ACE) Hog lung Purification  
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