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THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION
1. Evidence is presented that pepsin is a univalent acid with a value for pK of 6.85 (or a base, with pK 7.39). 2. The autodestruction of the pepsin is shown to be dependent in part upon an instantaneous irreversible change occurring in the ionized form of the enzyme (if it be an acid) or in the uni...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1927
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140918/ https://www.ncbi.nlm.nih.gov/pubmed/19872336 |
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author | Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph |
author_facet | Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph |
author_sort | Goulding, Arthur M. |
collection | PubMed |
description | 1. Evidence is presented that pepsin is a univalent acid with a value for pK of 6.85 (or a base, with pK 7.39). 2. The autodestruction of the pepsin is shown to be dependent in part upon an instantaneous irreversible change occurring in the ionized form of the enzyme (if it be an acid) or in the unionized form (if it be a base). 3. A further progressive autodestruction of pepsin at any given hydrogen ion concentration and temperature is defined by the mass law equation for a monomolecular reaction 4. The velocity of autodestruction of pepsin is directly proportional to the hydroxyl ion concentration. It is much less in the range of hydroxyl ion concentration from pOH 9.89-7.7, than in the range greater than pOH 7.7. In both of these ranges variations in pK with pOH may be represented by straight lines. |
format | Text |
id | pubmed-2140918 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1927 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21409182008-04-23 THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph J Gen Physiol Article 1. Evidence is presented that pepsin is a univalent acid with a value for pK of 6.85 (or a base, with pK 7.39). 2. The autodestruction of the pepsin is shown to be dependent in part upon an instantaneous irreversible change occurring in the ionized form of the enzyme (if it be an acid) or in the unionized form (if it be a base). 3. A further progressive autodestruction of pepsin at any given hydrogen ion concentration and temperature is defined by the mass law equation for a monomolecular reaction 4. The velocity of autodestruction of pepsin is directly proportional to the hydroxyl ion concentration. It is much less in the range of hydroxyl ion concentration from pOH 9.89-7.7, than in the range greater than pOH 7.7. In both of these ranges variations in pK with pOH may be represented by straight lines. The Rockefeller University Press 1927-01-20 /pmc/articles/PMC2140918/ /pubmed/19872336 Text en Copyright © Copyright, 1927, 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 Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION |
title | THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION |
title_full | THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION |
title_fullStr | THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION |
title_full_unstemmed | THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION |
title_short | THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION |
title_sort | autodestruction of pepsin in relation to its ionization |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140918/ https://www.ncbi.nlm.nih.gov/pubmed/19872336 |
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