Two Peaks in pH Dependence of Renin-angiotensinogen Reaction

• Published in: Bioscience, biotechnology, and biochemistry Vol. 62; no. 2; pp. 338 - 340
• Main Authors: NASIR, Uddin Mohammad, TAKAHASHI, Kohji, NAGAI, Takao, NAKAGAWA, Tsutomu, SUZUKI, Fumiaki, NAKAMURA, Yukio
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 1998; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Analytical, structural and metabolic biochemistry; Angiotensinogen - blood; Angiotensinogen - chemistry; Animals; Biological and medical sciences; Biotechnology; CHO Cells; Cricetinae; Enzyme-Linked Immunosorbent Assay; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Humans; Hydrogen-Ion Concentration; Hydrolases; Kinetics; pH dependence of renin; Rats; Recombinant Proteins - chemistry; Renin - analysis; Renin - chemistry; renin-angiotensinogen reaction; Sheep; Swine; two-peak pH dependence; Human; Enzyme; Environmental factor; In vitro; Peptidases; Renin angiotensin system; Renin; Angiotensinogen; Reaction mechanism; pH; Hydrolases; Aspartic endopeptidases; Kinetic parameter; Recombinant protein; Enzymatic reaction
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.62.338

The pH dependence of the reaction of purified recombinant human renin with purified recombinant sheep angiotensinogen was not a typical bell-shape but had two peaks, pH 6.4 and 8.9. The pH dependence of the reaction of human renin with human, hog, and rat angiotensinogens partially purified from plasma had a peak with a shoulder containing two peaks close together. These findings indicate that the reaction of renin with angiotensinogen involves at least two amino acid residues other than the two aspartic acid residues known to be involved and occurs at acidic pH and basic pH by two different pairs of these amino acid residues.