Preparative isolation of angiotensin-converting enzyme from human lung.
Angiotensin-converting enzyme from human lung was purified to apparent homogeneity using a five-step purification procedure consisting of ammonium sulfate precipitation, ion-exchange chromatography on DEAE Sephadex A-50, gel permeation on Sephadex G-200, chromatofocusing on a polybuffer exchange (PBE 94) column and high-performance liquid chromatographic gel permeation on a Bio-Sil TSK-250 column. This procedure gave an approximately 700-fold purification with a 20% yield compared to a 550-fold purification and a 1% yield with an affinity chromatography-based procedure. The 20-fold greater yield of the five-step procedure offers a major advantage for preparative use in the structural characterization of angiotensin-converting enzyme.
Meng
Q C
QC
Department of Cell Biology and Medicine, University of Alabama, Birmingham 35294.
King
S J
SJ
Branham
K E
KE
Delucas
L J
LJ
Lorber
B
B
Oparil
S
S
D015153:Blotting, Western; D002846:Chromatography, Affinity / Q000379:methods; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008168:Lung / Q000201:enzymology*; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification*
D007703:Peptidyl-Dipeptidase A