Partial purification and characterization of a renin-like enzyme from rat submandibular gland

摘要: Abstract A renin-like enzyme from rat submandibular gland was purified 40-fold by repeated chromatography on DEAE cellulose columns. The reaction product of this with a renin substrate plasma identified as angiotensin II paper chromatography, high voltage electrophoresis and radioimmunoassay. rate release is proportional to concentration, maximal between pH 5.8 6.1 obeys first order kinetics regard concentrations up 3200 ng/ml. generation declines during the incubation period, reaching almost zero at 30 min. variety possible causes for behaviour such angiotensinases, consumption, specificity, formation an inhibitor changes in conditions could be excluded. An unusual stimulation bifunctional SH reagents observed. Direct intravenous injection rats produced transient rise blood pressor, which differs qualitatively quantitatively that renin. It concluded clearly distinct well isorenin mouse gland. Comparison pseudorenin not due lack kinetic data latter enzyme.