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, Volume 6, Issue 4, pp 534–537 | Cite as

Biological and biochemical properties of angiotensin-converting enzyme

  • R. L. Soffer
  • M. Das
  • P. R. B. Caldwell
  • B. C. Seegal
  • K. C. Hsu
Article

Conclusions

Angiotensin-converting enzyme catalyzes cleavage of dipeptides from the COOH-termini of a large number of oligopeptides. It is a glycoprotein with a molecular weight of approximately 130,000 to 140,000 and contains a single, large polypeptide chain and one molar equivalent of bound zinc. It is located in blood vessel walls of many organs and is probably exposed on the luminal surface. It is also present in blood and certain parenchymal cells. Its two currently recognized important substrates are angiotensin I and bradykinin, and its action on each may be viewed as vasopressor. Thus, it catalyzes the formation of angiotensin II, a potent vasopressor agent, and the inactivation of bradykinin, a powerful vasodepressor molecule. The lung is important in regulating the level of angiotensin II in the systemic arterial circulation due to its strategic location, its large vascular bed and the fact that enzymatically generated angiotensin II is minimally metabolized in the pulmonary circulation. Studies with venom peptide inhibitors suggest that the enzyme may represent an important therapeutic target in renin-dependent hypertension. The enzyme is apparently accessible to exogenous anticatalytic antibody so that immunologic regulation of its activity may ultimately be feasible in vivo.

Keywords

Bradykinin Dipeptide Oligopeptides Peptide Inhibitor Blood Vessel Wall 

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Copyright information

© Birkhäuser-Verlag 1976

Authors and Affiliations

  • R. L. Soffer
    • 1
  • M. Das
    • 1
  • P. R. B. Caldwell
    • 2
  • B. C. Seegal
    • 2
  • K. C. Hsu
    • 2
  1. 1.Department of Molecular Biology, Division of Biological SciencesAlbert Einstein College of MedicineBronx
  2. 2.Departments of Medicine and Microbiology, College of Physicians and SurgeonsColumbia UniversityNew York

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