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THE PURIFICATION OF HYPERTENSIN I
The purification of hypertensin I has been described. The final product which is four times as powerful a pressor agent as l-arterenol, is obtained with an over-all recovery of 40 per cent. The product consists of a single component in countercurrent distribution, having a nitrogen content of 15.97...
| Autores principales: | , , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
The Rockefeller University Press
1954
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136385/ https://www.ncbi.nlm.nih.gov/pubmed/13201713 |
| _version_ | 1782143114934222848 |
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| author | Skeggs, Leonard T. Marsh, Walton H. Kahn, Joseph R. Shumway, Norman P. |
| author_facet | Skeggs, Leonard T. Marsh, Walton H. Kahn, Joseph R. Shumway, Norman P. |
| author_sort | Skeggs, Leonard T. |
| collection | PubMed |
| description | The purification of hypertensin I has been described. The final product which is four times as powerful a pressor agent as l-arterenol, is obtained with an over-all recovery of 40 per cent. The product consists of a single component in countercurrent distribution, having a nitrogen content of 15.97 per cent and a specific activity of 7050 Goldblatt units per mg. of N or 1125 units per mg. of solid. Acid hydrolysis and paper chromatography indicate in a preliminary fashion that there are about nine amino acids present in the intact polypeptide. |
| format | Text |
| id | pubmed-2136385 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 1954 |
| publisher | The Rockefeller University Press |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-21363852008-04-17 THE PURIFICATION OF HYPERTENSIN I Skeggs, Leonard T. Marsh, Walton H. Kahn, Joseph R. Shumway, Norman P. J Exp Med Article The purification of hypertensin I has been described. The final product which is four times as powerful a pressor agent as l-arterenol, is obtained with an over-all recovery of 40 per cent. The product consists of a single component in countercurrent distribution, having a nitrogen content of 15.97 per cent and a specific activity of 7050 Goldblatt units per mg. of N or 1125 units per mg. of solid. Acid hydrolysis and paper chromatography indicate in a preliminary fashion that there are about nine amino acids present in the intact polypeptide. The Rockefeller University Press 1954-09-30 /pmc/articles/PMC2136385/ /pubmed/13201713 Text en Copyright © Copyright, 1954, by The Rockefeller Institute for Medical Research New York 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 Skeggs, Leonard T. Marsh, Walton H. Kahn, Joseph R. Shumway, Norman P. THE PURIFICATION OF HYPERTENSIN I |
| title | THE PURIFICATION OF HYPERTENSIN I |
| title_full | THE PURIFICATION OF HYPERTENSIN I |
| title_fullStr | THE PURIFICATION OF HYPERTENSIN I |
| title_full_unstemmed | THE PURIFICATION OF HYPERTENSIN I |
| title_short | THE PURIFICATION OF HYPERTENSIN I |
| title_sort | purification of hypertensin i |
| topic | Article |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136385/ https://www.ncbi.nlm.nih.gov/pubmed/13201713 |
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