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Science 10 May 1963:
Vol. 140. no. 3567, pp. 672 - 674
DOI: 10.1126/science.140.3567.672

Articles

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

Philip A. Khairallah 1, F. Merlin Bumpus 1, Irvine H. Page 1, and Robert R. Smeby 1

1 Research Division, Cleveland Clinic Foundation, Cleveland, Ohio

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 beta-aspartyl1-angiotensin II, arginyl1-angiotensin II or deaminoangiotensin II. This enzyme, given the name angiotensinase A, requires agr-L-aspartic acid or agr-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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Kidney Aminopeptidase A and Hypertension, Part I : Spontaneously Hypertensive Rats.
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Kidney Aminopeptidase A and Hypertension, Part II : Effects of Angiotensin II.
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Renin in the Diagnosis of Renovascular Hypertension: Activity in Renal and Peripheral Vein Plasma.
B. M. Winer, W. F. Lubbe, M. Simon, and J. A. Williams (1967)
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Renal Erythropoietic Factor: Role of Ions and Vasoactive Agents in Erythropoietin Formation.
E. D. Zanjani, J. F. Contrera, G. W. Cooper, A. S. Gordon, and K. K. Wong (1967)
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Plasma Angiotensinase Activity in Hypertensive Patients.
H. D. Itskovitz, S. J. Dudrick, I. Dyrda, and J. J. Murphy (1967)
Arch Intern Med 119, 241-246
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Hypertensive Vascular Disease Produced by Homologous Renin.
G. M. C. Masson, C. Kashii, M. Matsunaga, and I. H. Page (1964)
Science 145, 178-180
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Renal Baroceptor Control of Renin Secretion.
S. L. Skinner, J. W. McCubbin, and I. H. Page (1963)
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