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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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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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creator	SANDER, GARY E HUGGINS, CLYDE G
description	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.
doi_str_mv	10.1038/newbio230027a0
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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. 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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.</description><subject>Acid Phosphatase - analysis</subject><subject>Angiotensin II - metabolism</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Centrifugation, Density Gradient</subject><subject>Electron Transport Complex IV - analysis</subject><subject>Endopeptidases - analysis</subject><subject>Female</subject><subject>Glucuronidase - analysis</subject><subject>L-Lactate Dehydrogenase - analysis</subject><subject>letters-to-editor</subject><subject>Life Sciences</subject><subject>Lung - cytology</subject><subject>Lung - enzymology</subject><subject>Male</subject><subject>Microsomes - enzymology</subject><subject>Mitochondria - enzymology</subject><subject>Rabbits</subject><subject>Sodium Chloride</subject><issn>0028-0836</issn><issn>0090-0028</issn><issn>1476-4687</issn><issn>2058-1092</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1971</creationdate><recordtype>article</recordtype><recordid>eNp1UE1LwzAYDqLMOb16E3oQb92SJm2To4ypk4Lgx7kk3duR0SYzaZXt15uxMVDw9L48X_A8CF0TPCaY8omBb6VtQjFOcolP0JCwPItZxvNTNAwgjzGn2Tm68H6FMU5JzgZowGiSccKG6PmtVxU0Td9IFxW2ko3eyk5bE9k6ujdLbTswXptoHk2t-QLXabOMZma7aSEK8KtUSndR0ZvlJTqrZePh6nBH6ONh9j59iouXx_n0vogrmoouplSpNGcp5RhTUsnw4WwhOE1TVSVQS0YEZCIAhCoQAgugKcHAeC5qUSd0hO72uWtnP3vwXdlqv-sgDdjelznjwZzjIBzvhZWz3juoy7XTrXSbkuByN175e7xguDkk96qFxVF-WCvwkz3vA2OW4MqV7Z0JZf9PvN07jOx6B8fEP7Ifh4GGzQ</recordid><startdate>19710303</startdate><enddate>19710303</enddate><creator>SANDER, GARY E</creator><creator>HUGGINS, CLYDE G</creator><general>Nature Publishing Group UK</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19710303</creationdate><title>Subcellular Localization of Angiotensin I Converting Enzyme in Rabbit Lung</title><author>SANDER, GARY E ; HUGGINS, CLYDE G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c359t-33bb5745380031ca45306d98355bc2efa419e6998313be9909e3510e4879f9f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1971</creationdate><topic>Acid Phosphatase - analysis</topic><topic>Angiotensin II - metabolism</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Centrifugation, Density Gradient</topic><topic>Electron Transport Complex IV - analysis</topic><topic>Endopeptidases - analysis</topic><topic>Female</topic><topic>Glucuronidase - analysis</topic><topic>L-Lactate Dehydrogenase - analysis</topic><topic>letters-to-editor</topic><topic>Life Sciences</topic><topic>Lung - cytology</topic><topic>Lung - enzymology</topic><topic>Male</topic><topic>Microsomes - enzymology</topic><topic>Mitochondria - enzymology</topic><topic>Rabbits</topic><topic>Sodium Chloride</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SANDER, GARY E</creatorcontrib><creatorcontrib>HUGGINS, CLYDE G</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SANDER, GARY E</au><au>HUGGINS, CLYDE G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Subcellular Localization of Angiotensin I Converting Enzyme in Rabbit Lung</atitle><jtitle>Nature (London)</jtitle><stitle>Nature New Biology</stitle><addtitle>Nat New Biol</addtitle><date>1971-03-03</date><risdate>1971</risdate><volume>230</volume><issue>9</issue><spage>27</spage><epage>29</epage><pages>27-29</pages><issn>0028-0836</issn><issn>0090-0028</issn><eissn>1476-4687</eissn><eissn>2058-1092</eissn><abstract>THE rapidity with which angiotensin I is converted to angiotensin II1-5 suggests that the subcellular localization of the converting enzyme is important. 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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
title	Subcellular Localization of Angiotensin I Converting Enzyme in Rabbit Lung
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