Angiotensin I converting enzyme from human plasma

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Abstract
The angiotensin I converting enzyme was purified 101,000-fold to homogeneity from human plasma by a combination of chromatographic and electrophoretic techniques. The enzyme is similar to other angiotensin I converting enzymes. It is an acidic glycoprotein consisting of a single polypeptide chain of MW 140,000 with an isoelectric point of 4.6. The enzyme requires Cl- for activity and is inhibited by EDTA, angiotensin II, bradykinin, bradykinin potentiating factor nonapeptide, and 3-mercapto-2-D-methylpropanoyl-L-proline (SQ-14,225). The purified preparation cleaves bradykinin and angiotensin I and hippuryl-L-histidyl-L-leucine. Its specific activity with angiotensin I is 2.4 units/mg and with hippuryl-L-histidyl-L-leucine is 31.4 units/mg.