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 un...

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Main Authors:	Goulding, Arthur M., Borsook, Henry, Wasteneys, Hardolph
Format:	Online
Language:	English
Published:	The Rockefeller University Press 1927
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140918/

id	pubmed-2140918
recordtype	oai_dc
spelling	pubmed-21409182008-04-23 THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph 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/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph
spellingShingle	Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION
author_facet	Goulding, Arthur M. Borsook, Henry Wasteneys, Hardolph
author_sort	Goulding, Arthur M.
title	THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION
title_short	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_sort	autodestruction of pepsin in relation to its ionization
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.
publisher	The Rockefeller University Press
publishDate	1927
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140918/
_version_	1611422502322438144

THE AUTODESTRUCTION OF PEPSIN IN RELATION TO ITS IONIZATION

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