Esther C R, Thomas K E, Bernstein K E
Department of Pathology and Laboratory Medicine, Emory University, Atlanta, GA 30322.
Biochem Biophys Res Commun. 1994 Dec 30;205(3):1916-21. doi: 10.1006/bbrc.1994.2894.
Chicken angiotensin converting enzyme (ACE) cDNA was cloned based on homology to the mouse ACE sequence. The chicken ACE protein is highly homologous to the somatic isozyme of ACE found in human, mouse, bovine, and rabbit. Like the mammalian somatic forms, the chicken enzyme consists of two putative zinc binding sites at the center of two homologous domains. All known functional residues are absolutely conserved. Unlike the mammals, no evidence for a single domain, testis specific form of ACE was found in the chicken testis by either Northern blot or enzyme assay. This result is unexpected since the adult mammalian testis expresses one of the highest tissue levels of ACE.
基于与小鼠ACE序列的同源性克隆了鸡血管紧张素转换酶(ACE)cDNA。鸡ACE蛋白与在人、小鼠、牛和兔中发现的ACE体细胞同工酶高度同源。与哺乳动物的体细胞形式一样,鸡的这种酶在两个同源结构域的中心由两个假定的锌结合位点组成。所有已知的功能残基都是绝对保守的。与哺乳动物不同,通过Northern印迹或酶分析在鸡睾丸中未发现单一结构域的、睾丸特异性形式的ACE的证据。这一结果出乎意料,因为成年哺乳动物睾丸中ACE的组织水平是最高的之一。