Tani M, Mizuno K, Hashimoto S, Niimura S, Yabe R, Kunii N, Suenaga K, Watari H, Fukuchi S
Clin Exp Hypertens A. 1987;9(2-3):267-71. doi: 10.3109/10641968709164186.
High activity of angiotensin-converting enzyme was demonstrated in human neuroblastoma tissue. This activity required the presence of chloride ion and was almost completely inhibited by a specific converting enzyme inhibitor captopril (10 nM), indicating that the activity measured is indeed angiotensin-converting enzyme. Furthermore, the biochemical features of the enzyme were closely similar to the well-known properties of human lung converting enzyme, such as molecular weight (290,000), optimum pH (8.0-8.5), the presence of glycoprotein residues, and dependence on chloride ion concentration. These results provide definitive evidence for the presence of true angiotensin-converting enzyme in human neuroblastoma tissue.
在人类神经母细胞瘤组织中证实了血管紧张素转换酶的高活性。这种活性需要氯离子的存在,并且几乎完全被特异性转换酶抑制剂卡托普利(10 nM)抑制,这表明所测得的活性确实是血管紧张素转换酶。此外,该酶的生化特性与人类肺转换酶的已知特性非常相似,如分子量(290,000)、最适pH(8.0 - 8.5)、糖蛋白残基的存在以及对氯离子浓度的依赖性。这些结果为人类神经母细胞瘤组织中存在真正的血管紧张素转换酶提供了确凿证据。