缩合单宁对血管紧张素转换酶的抑制作用。

Inhibitory effects of condensed tannins on angiotensin converting enzyme.

作者信息

Uchida S, Ikari N, Ohta H, Niwa M, Nonaka G, Nishioka I, Ozaki M

出版信息

Jpn J Pharmacol. 1987 Feb;43(2):242-6. doi: 10.1254/jjp.43.242.

DOI:10.1254/jjp.43.242

Abstract

Effects of condensed tannins isolated from Rhei Rhizoma on the activities of angiotensin converting enzyme (ACE) and various proteases were examined in vitro. Among the various condensed tannins tested, procyanidin B-5 3,3'-di-O-gallate and procyanidin C-1 3,3',3"-tri-O-gallate strongly inhibited the activity of ACE. The concentration of procyanidin B-5 3,3'-di-O-gallate required for 50% inhibition of ACE was 1.3 X 10(-6) M. The inhibition of ACE by condensed tannins was reversible and non-competitive, according to dialysis and to Dixon plots. However, over one hundred times the concentration was required to inhibit activities of other proteases such as trypsin, chymotrypsin, leucine aminopeptidase, carboxypeptidase A and urinary kallikrein. These results suggest that the inhibitory effects of condensed tannins on the activities of ACE are specific.

摘要

体外研究了从大黄根茎中分离得到的缩合单宁对血管紧张素转换酶（ACE）和各种蛋白酶活性的影响。在所测试的各种缩合单宁中，原花青素B-5 3,3'-二-O-没食子酸酯和原花青素C-1 3,3',3''-三-O-没食子酸酯强烈抑制ACE的活性。50%抑制ACE所需的原花青素B-5 3,3'-二-O-没食子酸酯浓度为1.3×10⁻⁶ M。根据透析和狄克逊图，缩合单宁对ACE 的抑制是可逆的且非竞争性的。然而，抑制其他蛋白酶如胰蛋白酶、胰凝乳蛋白酶、亮氨酸氨肽酶、羧肽酶A和尿激肽释放酶的活性则需要超过一百倍的浓度。这些结果表明缩合单宁对ACE活性的抑制作用具有特异性。