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CRYSTALLIZATION OF PEPSIN FROM ALCOHOL

1. Pepsin is soluble in 65 per cent alcohol and may be readily crystallized from 20 per cent alcohol. The crystals appear as needles or plates which may be transformed into the usual hexagonal bipyramids by recrystallization from water. The different crystals are probably two crystalline forms of th...

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Detalles Bibliográficos
Autor principal: Northrop, John H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1946
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142821/
https://www.ncbi.nlm.nih.gov/pubmed/19873485
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author Northrop, John H.
author_facet Northrop, John H.
author_sort Northrop, John H.
collection PubMed
description 1. Pepsin is soluble in 65 per cent alcohol and may be readily crystallized from 20 per cent alcohol. The crystals appear as needles or plates which may be transformed into the usual hexagonal bipyramids by recrystallization from water. The different crystals are probably two crystalline forms of the same chemical substance. 2. The enzyme is quite stable in 20 per cent alcohol at pH 2.0 but is inactivated by high concentrations of alcohol. 3. The enzyme is stable for several hours in 65 per cent alcohol at pH 4.0 to 5.0 but is rapidly inactivated in more acid solution. 4. No increase in activity could be noted after treatment with hydrogen peroxide. 5. No proteolytic activity either before or after treatment with hydrogen peroxide could be found in trichloracetic acid filtrates, butyl alcohol extracts of pepsin preparations, or oxidized phenylhydrazine solutions.
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spelling pubmed-21428212008-04-23 CRYSTALLIZATION OF PEPSIN FROM ALCOHOL Northrop, John H. J Gen Physiol Article 1. Pepsin is soluble in 65 per cent alcohol and may be readily crystallized from 20 per cent alcohol. The crystals appear as needles or plates which may be transformed into the usual hexagonal bipyramids by recrystallization from water. The different crystals are probably two crystalline forms of the same chemical substance. 2. The enzyme is quite stable in 20 per cent alcohol at pH 2.0 but is inactivated by high concentrations of alcohol. 3. The enzyme is stable for several hours in 65 per cent alcohol at pH 4.0 to 5.0 but is rapidly inactivated in more acid solution. 4. No increase in activity could be noted after treatment with hydrogen peroxide. 5. No proteolytic activity either before or after treatment with hydrogen peroxide could be found in trichloracetic acid filtrates, butyl alcohol extracts of pepsin preparations, or oxidized phenylhydrazine solutions. The Rockefeller University Press 1946-11-20 /pmc/articles/PMC2142821/ /pubmed/19873485 Text en Copyright © Copyright, 1946, 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.
CRYSTALLIZATION OF PEPSIN FROM ALCOHOL
title CRYSTALLIZATION OF PEPSIN FROM ALCOHOL
title_full CRYSTALLIZATION OF PEPSIN FROM ALCOHOL
title_fullStr CRYSTALLIZATION OF PEPSIN FROM ALCOHOL
title_full_unstemmed CRYSTALLIZATION OF PEPSIN FROM ALCOHOL
title_short CRYSTALLIZATION OF PEPSIN FROM ALCOHOL
title_sort crystallization of pepsin from alcohol
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142821/
https://www.ncbi.nlm.nih.gov/pubmed/19873485
work_keys_str_mv AT northropjohnh crystallizationofpepsinfromalcohol