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Angiotensin II, the potent hypertensive octapeptide, can be generated by a sequential cleavage of the carboxyl-terminal leucine and histidine from angiotensin I by a human renal extract. This extract does not hydrolyze further the resulting octapeptide. The more widely recognized biosynthetic pathway is by the extracellular dipeptide cleavage of angiotensin I by an enzyme which also degrades bradykinin, i.e., angiotensin converting enzyme. The presence of a carboxypeptidase activity capable of generating but not further hydrolyzing angiotensin II was observed in an ammonium sulfate fraction of a human renal extract. This novel enzymatic activity is distinct from angiotensin converting enzyme activity in that it is not dependent upon calcium and is not inhibited by known angiotensin converting enzyme inhibitors.
D G Changaris, and
J J Miller, and
R S Levy
June 1968,
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D G Changaris, and
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R S Levy
January 1991,
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D G Changaris, and
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R S Levy
January 1988,
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D G Changaris, and
J J Miller, and
R S Levy
December 1981,
Biochimica et biophysica acta,
D G Changaris, and
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R S Levy
April 2002,
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D G Changaris, and
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R S Levy
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D G Changaris, and
J J Miller, and
R S Levy
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D G Changaris, and
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R S Levy
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D G Changaris, and
J J Miller, and
R S Levy
December 1996,
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D G Changaris, and
J J Miller, and
R S Levy
December 1997,
Kidney international. Supplement,
