Gutkowska J, Corvol P, Thibault G, Genest J
Can J Biochem. 1982 Aug;60(8):843-6. doi: 10.1139/o82-106.
Tonin, a new serine protease, found in high concentration in rat submaxillary glands, leads to a significant activation of human amniotic fluid renin. The optimum pH on renin activation by tonin was found at pH 6.0. The reaction was time dependent and the initial rate of angiotensin I generation was constant up to 2 h. The two amniontic fluid samples studied showed an increase in renin activity after incubation with tonin to about five times the control level (268 to 1240 pmol x h-1 x mL-1 and 1490 to 7480 pmol x h-1 x mL-1).
托宁是一种新的丝氨酸蛋白酶，在大鼠下颌下腺中高浓度存在，可导致人羊水肾素显著激活。发现托宁激活肾素的最适pH值为6.0。该反应具有时间依赖性，在长达2小时内血管紧张素I生成的初始速率保持恒定。所研究的两份羊水样本在与托宁孵育后肾素活性增加至对照水平的约五倍（分别从268至1240 pmol·h⁻¹·mL⁻¹和1490至7480 pmol·h⁻¹·mL⁻¹）。
