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ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN
An enzyme with the characteristics of classical renin was isolated from brain extracts of nephrectomized dogs. This enzyme is thermolabile, nondialyzable, and forms a vasoconstrictive material when incubated with renin plasma substrate at pH 7. A short lasting pressor activity was also found in brai...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1971
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138896/ https://www.ncbi.nlm.nih.gov/pubmed/4332372 |
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author | Fischer-Ferraro, Catalina Nahmod, Victor E. Goldstein, Daniel J. Finkielman, Samuel |
author_facet | Fischer-Ferraro, Catalina Nahmod, Victor E. Goldstein, Daniel J. Finkielman, Samuel |
author_sort | Fischer-Ferraro, Catalina |
collection | PubMed |
description | An enzyme with the characteristics of classical renin was isolated from brain extracts of nephrectomized dogs. This enzyme is thermolabile, nondialyzable, and forms a vasoconstrictive material when incubated with renin plasma substrate at pH 7. A short lasting pressor activity was also found in brain extracts of dogs and rats. This activity was due to a substance identified by chemical and pharmacological tests as angiotensin. Countercurrent distribution of brain extracts of rats showed that 38% of the pressor activity corresponded to angiotensin II and the remainder to angiotensin I. A remarkable correlation was found between angiotensin and norepinphrine concentrations in different portions of the encephalon of the dog. |
format | Text |
id | pubmed-2138896 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1971 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21388962008-04-17 ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN Fischer-Ferraro, Catalina Nahmod, Victor E. Goldstein, Daniel J. Finkielman, Samuel J Exp Med Article An enzyme with the characteristics of classical renin was isolated from brain extracts of nephrectomized dogs. This enzyme is thermolabile, nondialyzable, and forms a vasoconstrictive material when incubated with renin plasma substrate at pH 7. A short lasting pressor activity was also found in brain extracts of dogs and rats. This activity was due to a substance identified by chemical and pharmacological tests as angiotensin. Countercurrent distribution of brain extracts of rats showed that 38% of the pressor activity corresponded to angiotensin II and the remainder to angiotensin I. A remarkable correlation was found between angiotensin and norepinphrine concentrations in different portions of the encephalon of the dog. The Rockefeller University Press 1971-01-31 /pmc/articles/PMC2138896/ /pubmed/4332372 Text en Copyright © 1971 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Fischer-Ferraro, Catalina Nahmod, Victor E. Goldstein, Daniel J. Finkielman, Samuel ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN |
title | ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN |
title_full | ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN |
title_fullStr | ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN |
title_full_unstemmed | ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN |
title_short | ANGIOTENSIN AND RENIN IN RAT AND DOG BRAIN |
title_sort | angiotensin and renin in rat and dog brain |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138896/ https://www.ncbi.nlm.nih.gov/pubmed/4332372 |
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