Purification of bovine angiotensin converting enzyme.
A change has been made in the commonly used lisinopril affinity gel procedure for purifying angiotensin converting enzyme. The new method greatly decreases the time required and greatly increases the yield of pure enzyme. All of the enzyme in various bovine tissues was extracted with 0.5% triton X-100 and applied to the affinity column; 70% was trapped and all of the trapped enzyme was released as the apoenzyme by EDTA. The holoenzyme was recovered by dialysis against zinc containing buffer. The turnover numbers were precisely the same for enzyme from lung, atrium, kidney, striatum and blood. The tissue concentrations of ACE were very different but the final specific activities were the same.
Schullek
J R
JR
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.
Wilson
I B
IB
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D003342:Corpus Striatum / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006325:Heart Atria / Q000032:analysis; D007668:Kidney / Q000032:analysis; D008168:Lung / Q000032:analysis; D007703:Peptidyl-Dipeptidase A / Q000097:blood / Q000302:isolation & purification*
D007703:Peptidyl-Dipeptidase A