Komissarova N V, Siems W E, Gomazkov O A, Oehme P, Jentzsch K D
Biull Eksp Biol Med. 1982 Jun;93(6):3-5.
Substance "P" (SP) and its derivatives inhibited activity of angiotensin-converting enzyme (ACE) in human blood serum, I50 for SP was 31 microM. The same results were obtained for N-terminal fragments of the SP molecule: Arg-Pro-Lys-Pro and Lys-Pro. The C-terminal heptapeptide and the dipeptide Arg-Pro negligibly inhibited ACE activity. A possible significance of the interaction between SP and ACE in the regulation of the microhemodynamics is discussed.
P物质（SP）及其衍生物可抑制人血清中血管紧张素转换酶（ACE）的活性，SP的半数抑制浓度（IC50）为31微摩尔。SP分子的N端片段：精氨酸-脯氨酸-赖氨酸-脯氨酸和赖氨酸-脯氨酸也得到了相同的结果。C端七肽和二肽精氨酸-脯氨酸对ACE活性的抑制作用可忽略不计。文中讨论了SP与ACE之间的相互作用在微循环动力学调节中的可能意义。
