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Abstract
A multistep procedure has been described for the purification of human renin from
cadaver kidneys. A 59-fold increase in specific activity from Step 1 through Step
4 occurs. The final product is reasonably stable when stored at pH 7.5 and −20 °C.
A high degree of purity is inferred from: (1) its appearance on polyacrylamide disc
gel electrophoresis, (2) the great increase in specific activity, and (3) the absence
of detectable angiotensinase activity beyond Step 3. A single band is seen on analytical
polyacrylamide disc gel electrophoresis after further purification of Step 4 renin
by preparative polyacrylamide gel electrophoresis, but a loss of biological activity
accompanies this procedure. Proof that the purified material is, indeed, renin is
provided by the following: (1) It increases linearly the renin activity of human plasma;
(2) incubation of this purified protein with human substrate produces a pressor substance
which is heat and acid stable, and which behaves like angiotensins I or II in the
rat bioassay; (3) assay of the pressor material by the radioimmunoassay method for
angiotensins I and II indicates that most of it can be accounted for as angiotensin
I. Finally, antibodies produced against this purified renin are effective in neutralizing
endogenous plasma renin activity. These findings suggest a very close resemblance
of the purified human renin to the natural circulating enzyme.
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References
- Extraction, purification and acetylation of human renin and the production of anti-renin to human renin.Arch. Biochem. Biphys. 1965; 110: 534
- Purification of human renin.Biochim. Biophys. Acta. 1966; 122: 289
- Protein measurement with the Folin phenol reagent.J. Biol. Chem. 1951; 193: 265
- Extraction, purification and assay of human renin free of angiotensinase.Circulation Res. 1966; 19: 739
Cohen, E. L., et al.: The measurement of plasma renin activity by radioimmunoassay of generated angiotensin I. In preparation.
- Disc electrophoresis.Ann. N. Y. Acad. Sci. 1964; 121: 321
- An apparatus for preparative temperature regulated polyacrylamide gel electrophoresis.Anal. Biochem. 1964; 9: 351
- Postural augmentation of plasma renin activity and aldosterone excretion in normal people.J. Clin. Invest. 1967; 46: 418
- Molecular weight of renin determined by Sephadex gel filtration.Acta Chem. Scand. 1962; 18: 2403
- Page I. McCublin J.W. Renal hypertension. Year Book Medical Publishers, Inc, Chicago1968
- Purification of pig renin.Biochem. J. 1966; 99: 708
- Antirenin in man and animals.Trans. Ass. Amer. Physicians. 1951; 1: 122
- Studies on antirenin.Amer. J. Physiol. 1954; 177: 55
- Induced changes in the antigenicity of renin and production of antirenin to homologus renin and to human renin.Canad. Med. Ass. J. 1964; 90: 236
- Antigenicity, solubility and clinical stability of renin complexes.J. Immun. 1961; 87: 472
Article info
Publication history
Accepted:
July 15,
1970
Received:
November 26,
1969
Footnotes
☆Supported in part by United States Public Health Service Grants AM-10257 and TI-AM-05501, National Institute of Arthritis and Metabolic Diseases, Grant No. 5M01 FR-4204 from the Division of Research Facilities and Resources, and by a grant from the University of Michigan Cancer Research Institute.
Identification
Copyright
© 1970 Published by Elsevier Inc.
