CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID

The decrease in protein nitrogen and in the activity of solutions of crystalline pepsin at pH 1.8 and 45°C. has been determined. The decrease in activity, as measured with eleven different methods, is in exact proportion to the decrease of protein nitrogen of the solution. The measurements were cont...

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Detalles Bibliográficos
Autor principal: Northrop, John H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1932
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2323772/
https://www.ncbi.nlm.nih.gov/pubmed/19872688
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author Northrop, John H.
author_facet Northrop, John H.
author_sort Northrop, John H.
collection PubMed
description The decrease in protein nitrogen and in the activity of solutions of crystalline pepsin at pH 1.8 and 45°C. has been determined. The decrease in activity, as measured with eleven different methods, is in exact proportion to the decrease of protein nitrogen of the solution. The measurements were continued until less than 5 per cent of the original protein remained. These results indicate that none of the split products of the protein molecule possess any appreciable activity compared to that of the original protein.
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spelling pubmed-23237722008-04-23 CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID Northrop, John H. J Gen Physiol Article The decrease in protein nitrogen and in the activity of solutions of crystalline pepsin at pH 1.8 and 45°C. has been determined. The decrease in activity, as measured with eleven different methods, is in exact proportion to the decrease of protein nitrogen of the solution. The measurements were continued until less than 5 per cent of the original protein remained. These results indicate that none of the split products of the protein molecule possess any appreciable activity compared to that of the original protein. The Rockefeller University Press 1932-09-20 /pmc/articles/PMC2323772/ /pubmed/19872688 Text en Copyright © Copyright, 1932, 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
Northrop, John H.
CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID
title CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID
title_full CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID
title_fullStr CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID
title_full_unstemmed CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID
title_short CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID
title_sort crystalline pepsin : iv. hydrolysis and inactivation by acid
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2323772/
https://www.ncbi.nlm.nih.gov/pubmed/19872688
work_keys_str_mv AT northropjohnh crystallinepepsinivhydrolysisandinactivationbyacid

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