Myara I, Marcon P, Lemonnier A, Chateliér B, Mangeot M
Clin Biochem. 1985 Aug;18(4):220-3. doi: 10.1016/s0009-9120(85)80043-6.
We describe prolinase (EC 3.4.13.8) activity in human plasma for the first time. Optimum activity was obtained with prolylvaline as substrate and 0.02 mmol/L manganese concentration at pH 9.0. Moreover, preincubation with manganese was not required, contrary to prolidase (EC 3.4.13.9) activity. The mean value observed in 106 subjects without liver and renal disorders was 16 U/L +/- 14 (2 SD). We determined this plasma enzyme activity in patients with acute hepatitis and chronic liver disease. Plasma prolinase activity was strongly dependent upon cytolysis because of the high activity in liver and the low activity in plasma. Of 24 patients with chronic liver disease (4 chronic hepatitis and 20 cirrhosis) and without cytolysis, prolinase activity was slightly increased in only three patients, whereas prolidase activity was increased in 13. This could be due to a difference in the activation of these two enzymes in liver during the fibrotic process.
我们首次描述了人血浆中的脯氨酰肽酶（EC 3.4.13.8）活性。以脯氨酰缬氨酸为底物，在pH 9.0、锰浓度为0.02 mmol/L的条件下可获得最佳活性。此外，与脯氨酰二肽酶（EC 3.4.13.9）活性相反，不需要用锰进行预孵育。在106名无肝脏和肾脏疾病的受试者中观察到的平均值为16 U/L +/- 14（2个标准差）。我们测定了急性肝炎和慢性肝病患者的这种血浆酶活性。由于肝脏中活性高而血浆中活性低，血浆脯氨酰肽酶活性强烈依赖于细胞溶解。在24例无细胞溶解的慢性肝病患者（4例慢性肝炎和20例肝硬化）中，只有3例患者的脯氨酰肽酶活性略有增加，而13例患者的脯氨酰二肽酶活性增加。这可能是由于在纤维化过程中肝脏中这两种酶的激活存在差异。
