Characterization of bovine atrial angiotensin-converting enzyme

被引:3
作者
Garats, EV
Nikolskaya, II
Binevski, PV
Pozdnev, VF
Kost, OA [1 ]
机构
[1] Moscow MV Lomonosov State Univ, Sch Chem, Moscow 119899, Russia
[2] Russian Acad Med Sci, Orekhovich Inst Biomed Chem, Moscow 119832, Russia
基金
俄罗斯基础研究基金会;
关键词
angiotensin converting enzyme; tissue specificity; bovine atrium; catalytic properties;
D O I
10.1023/A:1010205614096
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Bovine atrial angiotensin-converting enzyme (ACE) was purified to electrophoretic homogeneity. The purification procedure included ion-exchange chromatography on DEAE-Toyopearl 650M, affinity chromatography on lisinopril-agarose and eel filtration on Sephadex G-100. The bovine atrial ACE exhibited similar sensitivities to inhibition by lisinopril and captopril as lung AC E (the K,values for the atrial and lung enzymes differed insignificantly). However, the kinetic parameters of hydrolysis of some synthetic tripeptide substrates (FA-Phe-Gly-Gly, FA-Phe-Phe-Arg, Cbz-Phe-His-Leu, Hip-His-Leu) catalyzed by bovine atrial and lung ACE varied to a greater extent. The enzymes were also characterized by some differences in activation by chloride, nit rate, and sulfate an ions. These data support the hypothesis of tissue specificity of ACEs.
引用
收藏
页码:429 / 434
页数:6
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