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THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES
1. The tripeptide glycyl-levo-alanyl-glycine in solution of either one or ten equivalents of alkali does not undergo racemization on standing. 2. The dipeptide levo-alanyl-glycine under the conditions given in (1) does not undergo racemization. 3. In ketopiperazines, levo-alanyl-glycine anhydride an...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1925
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140749/ https://www.ncbi.nlm.nih.gov/pubmed/19872187 |
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author | Levene, P. A. Pfaltz, M. H. |
author_facet | Levene, P. A. Pfaltz, M. H. |
author_sort | Levene, P. A. |
collection | PubMed |
description | 1. The tripeptide glycyl-levo-alanyl-glycine in solution of either one or ten equivalents of alkali does not undergo racemization on standing. 2. The dipeptide levo-alanyl-glycine under the conditions given in (1) does not undergo racemization. 3. In ketopiperazines, levo-alanyl-glycine anhydride and in levo-prolyl-glycine anhydride under the influence of dilute alkalies, racemization takes place. 4. Racemization in the present experiments was never complete. The degree of racemization seems to depend, on the one hand, on the stability of the ketopiperazine ring; on the other, on the concentration of the alkali. 5. The significance of these observations will depend on the outcome of the work on a larger number of polypeptides and ketopiperazines. The work is now in progress in this laboratory. |
format | Text |
id | pubmed-2140749 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1925 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21407492008-04-23 THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES Levene, P. A. Pfaltz, M. H. J Gen Physiol Article 1. The tripeptide glycyl-levo-alanyl-glycine in solution of either one or ten equivalents of alkali does not undergo racemization on standing. 2. The dipeptide levo-alanyl-glycine under the conditions given in (1) does not undergo racemization. 3. In ketopiperazines, levo-alanyl-glycine anhydride and in levo-prolyl-glycine anhydride under the influence of dilute alkalies, racemization takes place. 4. Racemization in the present experiments was never complete. The degree of racemization seems to depend, on the one hand, on the stability of the ketopiperazine ring; on the other, on the concentration of the alkali. 5. The significance of these observations will depend on the outcome of the work on a larger number of polypeptides and ketopiperazines. The work is now in progress in this laboratory. The Rockefeller University Press 1925-09-18 /pmc/articles/PMC2140749/ /pubmed/19872187 Text en Copyright © Copyright, 1925, by The Rockefeller Institute for Medical Research 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 Levene, P. A. Pfaltz, M. H. THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES |
title | THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES |
title_full | THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES |
title_fullStr | THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES |
title_full_unstemmed | THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES |
title_short | THE ACTION OF ALKALIES ON PEPTIDES AND ON KETOPIPERAZINES |
title_sort | action of alkalies on peptides and on ketopiperazines |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140749/ https://www.ncbi.nlm.nih.gov/pubmed/19872187 |
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