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- W2023203999 abstract "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 enzyme with a purified renin substrate from rat plasma was identified as angiotensin II by paper chromatography, high voltage electrophoresis and radioimmunoassay. The rate of angiotensin release from substrate is proportional to enzyme concentration, is maximal between pH 5.8 and 6.1 and obeys first order kinetics with regard to substrate concentrations up to 3200 ng/ml. The rate of angiotensin generation declines during the incubation period, reaching almost zero at 30 min. A variety of possible causes for this behaviour such as angiotensinases, substrate consumption, substrate specificity, formation of an inhibitor and changes in the incubation conditions could be excluded. An unusual stimulation of the enzyme substrate reaction by bifunctional SH reagents was observed. Direct intravenous injection of the enzyme to rats produced a transient rise in blood pressor, which differs qualitatively and quantitatively from that produced by renin. It is concluded that the rat submandibular enzyme is clearly distinct from renin as well as from isorenin of mouse submandibular gland. Comparison with pseudorenin is not possible due to lack of kinetic data for the latter enzyme." @default.
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- W2023203999 title "Partial purification and characterization of a renin-like enzyme from rat submandibular gland" @default.
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- W2023203999 doi "https://doi.org/10.1016/0006-2952(72)90026-3" @default.
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