Depierre D, Bargetzi J P, Roth M
Enzyme. 1979;24(6):362-5. doi: 10.1159/000458691.
Several peptides were investigated for their inhibitory capacity against dipeptidyl carboxypeptidase (angiotensin-converting enzyme) from human seminal fluid. The strongest inhibitor was the nonapeptide SQ 20881. A marked inhibition was also shown by the compounds Phe-Ala-Pro and Boc-Phe-Ala-Pro, which behaved as competitive inhibitors. Among the peptides related to angiotensin, angiotensin III was the strongest inhibitor, followed by angiotensin II and the C-terminal hexapeptide of angiotensin II. The results indicate the dipeptidyl carboxypeptidase of human semen is very similar to pulmonary dipeptidyl carboxypeptidase in its susceptibility to peptide inhibitors. In view of these and other previously reported similarities, it is possible that both enzymes are identical.
研究了几种肽对人精液中二肽基羧肽酶(血管紧张素转换酶)的抑制能力。最强的抑制剂是九肽SQ 20881。化合物苯丙氨酸-丙氨酸-脯氨酸和叔丁氧羰基-苯丙氨酸-丙氨酸-脯氨酸也表现出显著的抑制作用,它们作为竞争性抑制剂。在与血管紧张素相关的肽中,血管紧张素III是最强的抑制剂,其次是血管紧张素II和血管紧张素II的C末端六肽。结果表明,人精液中的二肽基羧肽酶在对肽抑制剂的敏感性方面与肺二肽基羧肽酶非常相似。鉴于这些以及其他先前报道的相似性,这两种酶有可能是相同的。