MEASUREMENT OF HUMAN CONVERTING ENZYME LEVEL BY DIRECT RADIOIMMUNOASSAY

Abstract

CE [angiotensin I-converting enzyme] was purified from human lung, and antisera were raised in rabbits. Antisera inhibited the activity of the purified enzyme from lung and kidney and the plasma CE of normal persons and sarcoid patients. With antisera at a titer of 1:100,000, a sensitive, direct RIA [radioimmunoassay] was developed. CE purified from lung or kidney and CE present in normal and in sarcoid plasma gave parallel logit-log displacement lines, suggesting immunological identity. The level of CE in normal human plasma was 400 .+-. 131 ng/ml. In untreated sarcoid patients, the enzyme level and activity increased in parallel. There was a negative correlation (r = -0.81) between enzyme level and diffusing capacity of the lung for CO in sarcoid patients. Synthetic inhibitors such as captopril or MK 421 [enalapril maleate] did not interfere with the RIA, permitting enzyme levels to be monitored in [hypertensive] patients undergoing acute inhibitor therapy. During administration of MK 421, CE activity was negligible and plasma levels of CE did not change. In contrast, renin activity increased 8-fold during the inhibitor therapy.