Abstract
Three enzymes hydrolyzing angiotensin have been described in normal human plasma. Angiotensinase A 1 is an aminopeptidase requiring Ca ++ and a pH optimum of 7.4. It specifically hydrolyzes asparagine 1-angiotensin. Angiotensinase A 2 is also an aminopeptidase, requiring Ca ++ and has a pH optimum of 6.8. It specifically hydrolyzes aspartic acid 1-angiotensin. Angiotensinase B is an endopeptidase, requiring no cofactor with a pH optimum of 5.8 – 6.0. It hydrolyzes all angiotensin analogs studied and is inhibited by diisopropylfluorophosphate. Plasma angiotensinase activity usually measures angiotensinase A 1 since it is conducted at pH 7.4 with asparagine 1-angiotensin as substrate. In 133 hypertensive patients and 42 normal controls, no significant differences were found in the level of angiotensinase A 1 activity. Occasionally patients will be found whose plasma enzymes destroy angiotensin at increased rates possibly due to increase in nonspecific proteolytic enzymes.
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