ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN

It has been shown by the work presented in this paper that it is possible to dephosphorylate enzymically pepsin and pepsinogen with a variety of phosphatases. With the aid of a phosphodiesterase and the prostate phosphatase it has been established that the phosphorus in the two proteins is present a...

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Detalles Bibliográficos
Autor principal: Perlmann, Gertrude E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1958
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2194843/
https://www.ncbi.nlm.nih.gov/pubmed/13491815
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author Perlmann, Gertrude E.
author_facet Perlmann, Gertrude E.
author_sort Perlmann, Gertrude E.
collection PubMed
description It has been shown by the work presented in this paper that it is possible to dephosphorylate enzymically pepsin and pepsinogen with a variety of phosphatases. With the aid of a phosphodiesterase and the prostate phosphatase it has been established that the phosphorus in the two proteins is present as a diester and connects two sites of the peptide chain in a cyclic configuration. Removal of the phosphorus does not affect the proteolytic activity against hemoglobin or the synthetic substrate acetyl-L-phenylalanyl diiodotryosine, nor the pepsinogen pepsin transformation. However, an increase of the autodigestion of pepsin is observed.
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spelling pubmed-21948432008-04-23 ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN Perlmann, Gertrude E. J Gen Physiol Article It has been shown by the work presented in this paper that it is possible to dephosphorylate enzymically pepsin and pepsinogen with a variety of phosphatases. With the aid of a phosphodiesterase and the prostate phosphatase it has been established that the phosphorus in the two proteins is present as a diester and connects two sites of the peptide chain in a cyclic configuration. Removal of the phosphorus does not affect the proteolytic activity against hemoglobin or the synthetic substrate acetyl-L-phenylalanyl diiodotryosine, nor the pepsinogen pepsin transformation. However, an increase of the autodigestion of pepsin is observed. The Rockefeller University Press 1958-01-20 /pmc/articles/PMC2194843/ /pubmed/13491815 Text en Copyright © Copyright, 1958, 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
Perlmann, Gertrude E.
ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN
title ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN
title_full ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN
title_fullStr ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN
title_full_unstemmed ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN
title_short ENZYMIC DEPHOSPHORYLATION OF PEPSIN AND PEPSINOGEN
title_sort enzymic dephosphorylation of pepsin and pepsinogen
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2194843/
https://www.ncbi.nlm.nih.gov/pubmed/13491815
work_keys_str_mv AT perlmanngertrudee enzymicdephosphorylationofpepsinandpepsinogen

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