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ELECTROPHORESIS OF PEPSIN

1. A number of pepsin solutions containing several protein components have been studied by the electrophoresis method. All samples show a homogeneous boundary moving to the anode at pH 4.4. 2. The activity of this material may be higher than that of the original solution on the basis of total nitrog...

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Detalles Bibliográficos
Autores principales: Herriott, Roger M., Desreux, Victor, Northrop, John H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1940
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237938/
https://www.ncbi.nlm.nih.gov/pubmed/19873167
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author Herriott, Roger M.
Desreux, Victor
Northrop, John H.
author_facet Herriott, Roger M.
Desreux, Victor
Northrop, John H.
author_sort Herriott, Roger M.
collection PubMed
description 1. A number of pepsin solutions containing several protein components have been studied by the electrophoresis method. All samples show a homogeneous boundary moving to the anode at pH 4.4. 2. The activity of this material may be higher than that of the original solution on the basis of total nitrogen but is the same as that of the original solution on the basis of protein nitrogen. 3. There is no separation of the various protein components under these conditions. 4. The apparent isoelectric point at pH 2.7, previously obtained by the collodion particle method is due to the presence of decomposition products. Pure crystalline pepsin, free from decomposition products, is always negatively charged.
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spelling pubmed-22379382008-04-23 ELECTROPHORESIS OF PEPSIN Herriott, Roger M. Desreux, Victor Northrop, John H. J Gen Physiol Article 1. A number of pepsin solutions containing several protein components have been studied by the electrophoresis method. All samples show a homogeneous boundary moving to the anode at pH 4.4. 2. The activity of this material may be higher than that of the original solution on the basis of total nitrogen but is the same as that of the original solution on the basis of protein nitrogen. 3. There is no separation of the various protein components under these conditions. 4. The apparent isoelectric point at pH 2.7, previously obtained by the collodion particle method is due to the presence of decomposition products. Pure crystalline pepsin, free from decomposition products, is always negatively charged. The Rockefeller University Press 1940-03-20 /pmc/articles/PMC2237938/ /pubmed/19873167 Text en Copyright © Copyright, 1940, 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
Herriott, Roger M.
Desreux, Victor
Northrop, John H.
ELECTROPHORESIS OF PEPSIN
title ELECTROPHORESIS OF PEPSIN
title_full ELECTROPHORESIS OF PEPSIN
title_fullStr ELECTROPHORESIS OF PEPSIN
title_full_unstemmed ELECTROPHORESIS OF PEPSIN
title_short ELECTROPHORESIS OF PEPSIN
title_sort electrophoresis of pepsin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237938/
https://www.ncbi.nlm.nih.gov/pubmed/19873167
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