Isorenin, pseudorenin, cathepsin D and renin. A comparative enzymatic study of angiotensin-forming enzymes
E Hackenthal, R Hackenthal, U Hilgenfeldt - Biochimica et Biophysica Acta …, 1978 - Elsevier
1. Renin was purified 30 000-fold from rat kidneys by chromatography on DEAE-cellulose
and SP-Sephadex, and by affinity chromatography on pepstatinyl-Sepharose. 2. 2. The
enzymatic properties of isorenin from rat brain, pseudorenin from hog spleen, cathepsin D
from bovine spleen, and renin from rat kidneys were compared: Isorenin, pseudorenin and
cathepsin D generate angiotensin from tetradecapeptide renin substrate with pH optima
around 4.9, renin at 6.0. With sheep angiotensinogen as substrate, isorenin, pseudorenin …
and SP-Sephadex, and by affinity chromatography on pepstatinyl-Sepharose. 2. 2. The
enzymatic properties of isorenin from rat brain, pseudorenin from hog spleen, cathepsin D
from bovine spleen, and renin from rat kidneys were compared: Isorenin, pseudorenin and
cathepsin D generate angiotensin from tetradecapeptide renin substrate with pH optima
around 4.9, renin at 6.0. With sheep angiotensinogen as substrate, isorenin, pseudorenin …
