title: Brain renin from bovine anterior pituitary. Isolation and properties.
abstract: Brain renin has been purified 1,670,000-fold to homogeneity from bovine anterior pituitary in seven steps, including affinity chromatography on pepstatin-aminohexyl-agarose. The molecular weight of this enzyme is 36,000 as determined by gel filtration on Ultrogel AcA 44 and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme has an isoelectric point of 5.25 and works best at physiological pH. In contrast to renal renin, bovine brain renin fails to bind to concanavalin A and four other lectins. The angiotensin I-forming activity of the purified brain renin was completely neutralized by anti-hog renal renin antibody. Rabbit antisera against pure brain renin showed a low degree of species and tissue specificity, reacting readily with hog brain renin and bovine and hog kidney renins. These results provide definite evidence for the presence of a functional brain renin-angiotensin system.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000936:Antigen-Antibody Complex; D002417:Cattle; D002846:Chromatography, Affinity; D006863:Hydrogen-Ion Concentration; D007106:Immune Sera; D007700:Kinetics; D010903:Pituitary Gland, Anterior / Q000201:enzymology*; D012083:Renin / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D000596:Amino Acids; D000936:Antigen-Antibody Complex; D007106:Immune Sera; D012083:Renin