Purification of the Angiotensin I Converting Enzyme of the Lung.
OKLAHOMA UNIV HEALTH SCIENCES CENTER OKLAHOMA CITY
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The angiotensin I converting enzyme peptidyl dipeptide hydrolase was purified from hog lung. The molecular weight of the enzyme in SDS polyacrylamide gel electrophoresis was established as 206,000. The pI in isoelectrofocusing was found to be 4.3. The purified enzyme cleaved Bz-Gly-Gly-Gly and bradykinin. It was inhibited by a high concentration of urea and by the nonapeptide SQ 20881. Both compounds inhibited reversibly as shown in studies done with the water-insoluble Sepharose-converting enzyme complex. After gel filtration on a Sephadex G-200 column two additional forms of converting enzyme were detected. Author