Affinity chromatography of angiotensin I-converting enzyme from rabbit lung using hippurylhistidylleucyl-OH.
Approximately 50-fold purification of angiotensin I-converting enzyme (Peptidyldipeptide hydrolase, EC 3.4.15.1) from rabbit lung was achieved by affinity chromatography using the synthetic substrate Hippuryl-His-Leu-OH. The specific activity of the enzyme was increased from 0.044 units/mg protein to 1.911 units/mg protein for Hippuryl-His-Leu-OH and from 0.33 nmol/min per mg protein to 13.8 nmol/min per mg protein for angiotensin I.
D000804:Angiotensin II / Q000378:metabolism; D000818:Animals; D002846:Chromatography, Affinity; D006626:Hippurates; D006639:Histidine; D007930:Leucine; D008168:Lung / Q000201:enzymology*; D009842:Oligopeptides; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification*; D011817:Rabbits; D012685:Sepharose
D006626:Hippurates; D009842:Oligopeptides; D000804:Angiotensin II; C010980:hippuryl-histidyl-leucine; D006639:Histidine; D012685:Sepharose; D007703:Peptidyl-Dipeptidase A; D007930:Leucine