Abstract
AFTER the demonstration of two forms of angiotensin by Skeggs et al.1 and their preparation of an enzyme capable of catalysing the conversion of angiotensin I to angiotensin II (converting enzyme) from horse plasma2, attention centred round the blood as the physiologically significant site of converting enzyme. But when Ng and Vane3 showed that angiotensin I was converted to angiotensin II in the lungs and that the rate of conversion was sufficient to account for most of the conversion during a single passage through the circulation, attention was directed towards the lung. Bakhle4 partially purified the converting enzyme from dog lung but this preparation contained too much angiotensinase activity for extensive analysis of the converting enzyme to be possible. There have been several further studies of the conversion of angiotensin I to angiotensin II by extracts from various animal sources5–8, including the purification of converting enzyme from hog plasma9. We have now obtained a preparation of the enzyme from dog lung with only slight contamination by angiotensinase and have studied its characteristics with particular emphasis on its ionic requirements.
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References
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BAKHLE, Y., REYNARD, A. Characteristics of the Angiotensin I Converting Enzyme from Dog Lung. Nature New Biology 229, 187–189 (1971). https://doi.org/10.1038/newbio229187a0
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DOI: https://doi.org/10.1038/newbio229187a0
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