Renin and Angiotensin‐Converting Enzyme in Human Neuroblastoma Tissue

Abstract
High activity of renin was demonstrated in human neuroblastoma tissue. This activity was inhibited by specific antibody raised against human renal renin, indicating that it was not due to the nonspecific action of proteases. The specific activity of renin was 122.8 ng of angiotensin I generated/mg of protein/h-1. It shared some biochemical features with well-known kidney renin, such as MW, optimum pH, the presence of trypsin-activatable inactive renin and glycoprotein nature. Angiotensin-converting enzyme (ACE) activity (2.64 nmol mg of protein-1 min-1) was found in the tissue. This activity was inhibited by captopril, a specific ACE inhibitor or by omission of chloride ion. True renin in addition to ACE evidently exists in human neuroblastoma tissue.