Le Morvan P, Palaic D, Ferguson D
Can J Physiol Pharmacol. 1977 Jun;55(3):652-7. doi: 10.1139/y77-089.
The angiotensinase (EC 3.4.99.3) activity of the subcellular fractions of guinea pig aorta has been studied in relation to their [14C]angiotensin binding capacity. The enzyme activity occurs in the following decreasing order: supernatant greater than plasma membrane fraction greater than 105 000 X g pellet greater than mitochondrial fraction. The specific binding of [14C]angiotensin to these fractions follows the same pattern. Pretreatment of the subcellular fractions at 47 degrees C for 20 min was performed in an attempt to differentiate binding of angiotensin to the pharmacological receptor from binding to the destroying enzymes. This procedure decreased the angiotensinase activity in the plasma membrane fraction only whereas the specific binding of [14C]angiotensin to this fraction was not significantly decreased, suggesting that the plasma membrane angiotensinase is a thermolabile enzyme.
已研究了豚鼠主动脉亚细胞组分的血管紧张素酶（EC 3.4.99.3）活性与其[14C]血管紧张素结合能力的关系。酶活性按以下降序排列：上清液＞质膜组分＞105 000×g沉淀＞线粒体组分。[14C]血管紧张素与这些组分的特异性结合遵循相同模式。对亚细胞组分在47℃预处理20分钟，试图区分血管紧张素与药理受体的结合和与破坏酶的结合。该程序仅降低了质膜组分中的血管紧张素酶活性，而[14C]血管紧张素与该组分的特异性结合并未显著降低，这表明质膜血管紧张素酶是一种热不稳定酶。
