[人肝脏血管紧张素转换酶的纯化及其理化性质研究]

[Purification and study of the physicochemical properties of angiotensin converting enzyme from the human liver].

作者信息

Sakharov I Iu, Danilov S M, Sukhova N V

出版信息

Biull Eksp Biol Med. 1987 Mar;103(3):308-10.

Abstract

Angiotensin-converting enzyme (ACE) from human liver was first purified 9000-fold by chromatofocusing with 22% yield. The enzyme had a specific activity of 10 U/mg. The enzyme molecular weight was 150000, as determined by electrophoresis in a 7.5% polyacrylamide gel. The enzyme pI determined by chromatofocusing was 4.2-4.3. KM of human liver ACE, measured using hippuryl-L-histidyl-L-leucine and N-benzyloxycarbonyl-L-phenylalanyl-L-histidyl-L-leucine as substrates, was 5 mM and 0.1 mM, respectively. Human liver ACE was inhibited by SQ 20881 with IC50 equal to 1.8 X 10(-8) M.

摘要

人肝脏中的血管紧张素转换酶（ACE）首次通过色谱聚焦法纯化了9000倍，产率为22%。该酶的比活性为10 U/mg。通过在7.5%聚丙烯酰胺凝胶中电泳测定，该酶的分子量为150000。通过色谱聚焦法测定的该酶的pI为4.2 - 4.3。以马尿酰-L-组氨酰-L-亮氨酸和N-苄氧羰基-L-苯丙氨酰-L-组氨酰-L-亮氨酸为底物测定的人肝脏ACE的KM分别为5 mM和0.1 mM。人肝脏ACE被SQ 20881抑制，IC50等于1.8×10^(-8) M。