Changaris D G, Miller J J, Levy R S
Biochem Biophys Res Commun. 1986 Jul 31;138(2):573-9. doi: 10.1016/s0006-291x(86)80535-6.
Angiotensin II, the potent hypertensive octapeptide, can be generated by a sequential cleavage of the carboxyl-terminal leucine and histidine from angiotensin I by a human renal extract. This extract does not hydrolyze further the resulting octapeptide. The more widely recognized biosynthetic pathway is by the extracellular dipeptide cleavage of angiotensin I by an enzyme which also degrades bradykinin, i.e., angiotensin converting enzyme. The presence of a carboxypeptidase activity capable of generating but not further hydrolyzing angiotensin II was observed in an ammonium sulfate fraction of a human renal extract. This novel enzymatic activity is distinct from angiotensin converting enzyme activity in that it is not dependent upon calcium and is not inhibited by known angiotensin converting enzyme inhibitors.
血管紧张素II是一种强效的八肽高血压因子，可通过人肾提取物依次从血管紧张素I的羧基末端切割亮氨酸和组氨酸而生成。该提取物不会进一步水解生成的八肽。更广泛认可的生物合成途径是通过一种酶对血管紧张素I进行细胞外二肽切割，该酶也会降解缓激肽，即血管紧张素转换酶。在人肾提取物的硫酸铵级分中观察到一种羧肽酶活性，它能够生成血管紧张素II，但不会进一步水解它。这种新的酶活性与血管紧张素转换酶活性不同，因为它不依赖于钙，也不受已知的血管紧张素转换酶抑制剂的抑制。
