Hohlbrugger G, Schweisfurth H, Dahlheim H
J Reprod Fertil. 1982 May;65(1):97-103. doi: 10.1530/jrf.0.0650097.
Angiotensin I converting enzyme (ACE) was found in the testis, epididymis and vas deferens of rats. In tissue specimens without a prior washout of seminal fluid the highest specific ACE activity was measured in the testis. The enzyme activity was significantly lower towards the end of the excurrent ducts, suggesting that the enzyme is synthesized in the testis and secreted into the seminal fluid there. An ACE inhibiting substance may be secreted by the epididymal epithelium. Enzyme synthesis and enzyme inhibition are probably under simultaneous endocrine control. In-vitro inhibition, pH- and temperature-dependence of gonadal ACE correspond with that of lung and blood plasma. However, the physiological function of the enzyme on sperm motility and fertility remains unsolved.
在大鼠的睾丸、附睾和输精管中发现了血管紧张素I转换酶（ACE）。在未预先冲洗精液的组织标本中，睾丸中的ACE比活性最高。在输出管道末端，酶活性显著降低，这表明该酶在睾丸中合成并分泌到精液中。附睾上皮可能分泌一种ACE抑制物质。酶的合成和抑制可能同时受内分泌控制。性腺ACE的体外抑制、pH和温度依赖性与肺和血浆中的情况一致。然而，该酶对精子活力和生育能力的生理功能仍未明确。
