ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR

A method has been described for the isolation and crystallization of swine pepsin inhibitor from swine pepsinogen. Solubility experiments and fractional recrystallization show no drift in specific activity. The reversible combination of pepsin with the inhibitor was found to obey the mass law. The i...

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Detalles Bibliográficos
Autor principal: Herriott, Roger M.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1941
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237976/
https://www.ncbi.nlm.nih.gov/pubmed/19873219
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author Herriott, Roger M.
author_facet Herriott, Roger M.
author_sort Herriott, Roger M.
collection PubMed
description A method has been described for the isolation and crystallization of swine pepsin inhibitor from swine pepsinogen. Solubility experiments and fractional recrystallization show no drift in specific activity. The reversible combination of pepsin with the inhibitor was found to obey the mass law. The inhibitor is quite specific, failing to act on other proteolytic and milk clotting enzymes. The inhibitor is destroyed by pepsin at pH 3.5. Chemical and physical studies indicate that the inhibitor is a polypeptide of approximately 5,000 molecular weight with an isoelectric point at pH 3.7. It contains arginine, tyrosine, but no tryptophane and has basic groups in its structure.
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spelling pubmed-22379762008-04-23 ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR Herriott, Roger M. J Gen Physiol Article A method has been described for the isolation and crystallization of swine pepsin inhibitor from swine pepsinogen. Solubility experiments and fractional recrystallization show no drift in specific activity. The reversible combination of pepsin with the inhibitor was found to obey the mass law. The inhibitor is quite specific, failing to act on other proteolytic and milk clotting enzymes. The inhibitor is destroyed by pepsin at pH 3.5. Chemical and physical studies indicate that the inhibitor is a polypeptide of approximately 5,000 molecular weight with an isoelectric point at pH 3.7. It contains arginine, tyrosine, but no tryptophane and has basic groups in its structure. The Rockefeller University Press 1941-01-20 /pmc/articles/PMC2237976/ /pubmed/19873219 Text en Copyright © Copyright, 1941, 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
Herriott, Roger M.
ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR
title ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR
title_full ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR
title_fullStr ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR
title_full_unstemmed ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR
title_short ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR
title_sort isolation, crystallization, and properties of pepsin inhibitor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237976/
https://www.ncbi.nlm.nih.gov/pubmed/19873219
work_keys_str_mv AT herriottrogerm isolationcrystallizationandpropertiesofpepsininhibitor

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