Subcellular Localization of Angiotensin I Converting Enzyme in Rabbit Lung

THE rapidity with which angiotensin I is converted to angiotensin II1-5 suggests that the subcellular localization of the converting enzyme is important. Bakhle6 and Cushman and Cheung7 have demonstrated the particulate nature of this enzyme. Subcellular distribution studies and marker enzyme analys...

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Bibliographic Details
Published in:Nature (London) 1971-03, Vol.230 (9), p.27-29
Main Authors: SANDER, GARY E, HUGGINS, CLYDE G
Format: Article
Language:English
Subjects:
Acid Phosphatase - analysis
Angiotensin II - metabolism
Animals
Biomedical and Life Sciences
Centrifugation, Density Gradient
Electron Transport Complex IV - analysis
Endopeptidases - analysis
Female
Glucuronidase - analysis
L-Lactate Dehydrogenase - analysis
letters-to-editor
Life Sciences
Lung - cytology
Lung - enzymology
Male
Microsomes - enzymology
Mitochondria - enzymology
Rabbits
Sodium Chloride
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Summary:THE rapidity with which angiotensin I is converted to angiotensin II1-5 suggests that the subcellular localization of the converting enzyme is important. Bakhle6 and Cushman and Cheung7 have demonstrated the particulate nature of this enzyme. Subcellular distribution studies and marker enzyme analysis indicate that converting enzyme activity in rabbit lung is most concentrated in the pellet sedimenting at between 1,000 and 25,000g (P2), subsequently characterized as the light and heavy mitochondrial fraction. To identify this fraction more fully, we have resuspended P2 and centrifuged it through a discontinuous density gradient, a procedure which separates converting enzyme activity from the mitochondria. Marker enzyme analysis and electron microscopy suggest plasma membrane as the major constituent of that fraction displaying highest specific activity of converting enzyme.
ISSN:0028-0836
0090-0028
1476-4687
2058-1092
DOI:10.1038/newbio230027a0