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. 1974 May;71(5):1720–1724. doi: 10.1073/pnas.71.5.1720

Angiotensin-Converting Enzyme from Rabbit Pulmonary Particles

R L Soffer *, R Reza ‡, P R B Caldwell ‡
PMCID: PMC388310  PMID: 4365761

Abstract

Angiotensin-converting enzyme has been solubilized from rabbit pulmonary particles and purified to homogeneity. The molecular weight of the native enzyme was estimated to be about 136,000 by glycerol gradient centrifugation, and a value of 140,000 was obtained for the reduced denatured protein by disc-gel electrophoresis in the presence of sodium dodecyl sulfate and 2-mercaptoethanol. The enzyme was found to be a glycoprotein with carbohydrate accounting for approximately 16% of its dry weight. The major sugar residues were identified as galactose, N-acetylglucosamine, and mannose, with smaller amounts of fucose and sialic acid. The homogeneous enzyme catalyzed the release of His-Leu from the COOH-terminus of angiotensin I and of Phe-Arg and Ser-Pro from that of bradykinin.

Keywords: glycoprotein, hypertension

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bakhle Y. S. Conversion of angiotensin I to angiotensin II by cell-free extracts of dog lung. Nature. 1968 Nov 30;220(5170):919–921. doi: 10.1038/220919a0. [DOI] [PubMed] [Google Scholar]
  3. Baum S. G., Horwitz M. S., Maizel J. V., Jr Studies of the mechanism of enhancement of human adenovirus infection in monkey cells by simian virus 40. J Virol. 1972 Aug;10(2):211–219. doi: 10.1128/jvi.10.2.211-219.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cheung H. S., Cushman D. W. Inhibition of homogeneous angiotensin-converting enzyme of rabbit lung by synthetic venom peptides of Bothrops jararaca. Biochim Biophys Acta. 1973 Feb 15;293(2):451–463. doi: 10.1016/0005-2744(73)90352-5. [DOI] [PubMed] [Google Scholar]
  5. Codington J. F., Sanford B. H., Jeanloz R. W. Glycoprotein coat of the TA3 cell. Isolation and partial characterization of a sialic acid containing glycoprotein fraction. Biochemistry. 1972 Jul 4;11(14):2559–2564. doi: 10.1021/bi00764a001. [DOI] [PubMed] [Google Scholar]
  6. Cushman D. W., Cheung H. S. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem Pharmacol. 1971 Jul;20(7):1637–1648. doi: 10.1016/0006-2952(71)90292-9. [DOI] [PubMed] [Google Scholar]
  7. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  8. Dorer F. E., Kahn J. R., Lentz K. E., Levine M., Skeggs L. T. Purification and properties of angiotensin-converting enzyme from hog lung. Circ Res. 1972 Sep;31(3):356–366. doi: 10.1161/01.res.31.3.356. [DOI] [PubMed] [Google Scholar]
  9. Elisseeva Y. E., Orekhovich V. N., Pavlikhina L. V., Alexeenko L. P. Carboxycathepsin--a key regulatory component of two physiological systems involved in regulation of blood pressure. Clin Chim Acta. 1971 Feb;31(2):413–419. doi: 10.1016/0009-8981(71)90412-8. [DOI] [PubMed] [Google Scholar]
  10. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  11. Ferreira S. H., Greene L. H., Alabaster V. A., Bakhle Y. S., Vane J. R. Activity of various fractions of bradykinin potentiating factor against angiotensin I converting enzyme. Nature. 1970 Jan 24;225(5230):379–380. doi: 10.1038/225379a0. [DOI] [PubMed] [Google Scholar]
  12. Krieger E. M., Salgado H. C., Assan C. J. Greene LL, Ferreira SH: Potential screening test for detection of overactivity of renin-angiotensin system. Lancet. 1971 Feb 6;1(7693):269–271. doi: 10.1016/s0140-6736(71)91005-1. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  15. Miller E. D., Jr, Samuels A. I., Haber E., Barger A. C. Inhibition of angiotensin conversion in experimental renovascular hypertension. Science. 1972 Sep 22;177(4054):1108–1109. doi: 10.1126/science.177.4054.1108. [DOI] [PubMed] [Google Scholar]
  16. Ng K. K., Vane J. R. Conversion of angiotensin I to angiotensin II. Nature. 1967 Nov 25;216(5117):762–766. doi: 10.1038/216762a0. [DOI] [PubMed] [Google Scholar]
  17. SKEGGS L. T., Jr, KAHN J. R., SHUMWAY N. P. The preparation and function of the hypertensin-converting enzyme. J Exp Med. 1956 Mar 1;103(3):295–299. doi: 10.1084/jem.103.3.295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  19. Smith U., Ryan J. W. Electron microscopy of endothelial and epithelial components of the lungs: correlations of structure and function. Fed Proc. 1973 Sep;32(9):1957–1966. [PubMed] [Google Scholar]
  20. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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