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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...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1940
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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. |
format | Text |
id | pubmed-2237938 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1940 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT herriottrogerm electrophoresisofpepsin AT desreuxvictor electrophoresisofpepsin AT northropjohnh electrophoresisofpepsin |