PURIFICATION AND CHARACTERIZATION OF RED CELL ANGIOTENSINASE

Erythrocyte angiotensinase was obtained by hemolysis and concentrated 5 to 10 fold by sephadex gel filtration. Using the rat bioassay, the enzyme activity was determined as the half time of the degradation rate of angiotensin. Enzymatic activity was characterized with respect to the influence of pH, temperature and various concentrations of different salts. With progressively increasing concentrations of NaCl, KCl and CaCl2, the activity of angiotensinase reaches a maximum and then recedes. Such maxima were not obtained with CdCl2 and Hg2Cl2, rather, a complete inhibition of enzyme activity was noted. When the enzymatic degradation rate of hypertensin (CIBA) was compared with that of natural angiotensin, the degradation rate of the synthetic substance was approximately 6 times faster. © 1969 Springer-Verlag.