Reports

Angiotensinase with a High Degree of Specificity in Plasma and Red Cells

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Science  10 May 1963:
Vol. 140, Issue 3567, pp. 672-674
DOI: 10.1126/science.140.3567.672

Abstract

A peptidase with a high degree of specificity for angiotensin II occurs in normal human plasma and red cells. Preparations from both sources have the same pH optimum, require calcium ions, and hydrolyze valyl5- or isoleucyl5-angiotensin II, but do not hydrolyze β-aspartyl1-angiotensin II, arginyl1-angiotensin II or deaminoangiotensin II. This enzyme, given the name angiotensinase A, requires α-L-aspartic acid or α-L-asparagine as the N-terminal amino acid in its angiotensin substrate, and thus differs from kidney leucine aminopeptidase. Other peptidases known to hydrolyze angiotensin also hydrolyze at least one of the other angiotensin analogs with substitution in the one position.

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