Grisé C, Boucher R, Thibault G, Genest J
Can J Biochem. 1981 Apr;59(4):250-5. doi: 10.1139/o81-034.
The renin substrate (angiotensinogen) has been purified from outdated human blood bank plasma. A 100-fold purification was achieved by ammonium sulphate protein fractionation and four successive chromatographic procedures. We show that tonin, a serine protease enzyme found in submaxillary glands of the rat, cleaves the human plasma angiotensinogen, devoid of tonin inhibiting factor(s), at a pH optimum of 5--5.5. It generates a pressor substance that was identified as angiotensin (A) II. The rate of cleavage of the human angiotensinogen preparation by 1 nmol of renin or tonin was calculated to be 1320 nmol AI/h for renin and 26 nmol AII/h for tonin.
肾素底物（血管紧张素原）已从过期的人类血库血浆中纯化出来。通过硫酸铵蛋白分级分离和四个连续的色谱程序实现了100倍的纯化。我们发现，在大鼠颌下腺中发现的一种丝氨酸蛋白酶——托宁，在最适pH值为5-5.5时，可切割不含托宁抑制因子的人血浆血管紧张素原。它产生一种升压物质，被鉴定为血管紧张素（A）II。计算得出，1 nmol肾素或托宁对人血管紧张素原制剂的切割速率，肾素为1320 nmol AI/h，托宁为26 nmol AII/h。
