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Pepsinogen and Pepsin
Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1962
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195218/ https://www.ncbi.nlm.nih.gov/pubmed/13906833 |
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author | Herriott, Roger M. |
author_facet | Herriott, Roger M. |
author_sort | Herriott, Roger M. |
collection | PubMed |
description | Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is initiated by a peptic cleavage of the protein chain, a single enzymic site is formed. This site is made up, quite probably, of the secondary carboxyl group of glutamic acid or of aspartic acid and a tyrosine phenol group in close proximity so that they can form hydrogen or hydrophobic bonds with the substrate in some unique manner that permits hydrolysis to occur at an accelerated rate. |
format | Text |
id | pubmed-2195218 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1962 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21952182008-04-23 Pepsinogen and Pepsin Herriott, Roger M. J Gen Physiol Article Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is initiated by a peptic cleavage of the protein chain, a single enzymic site is formed. This site is made up, quite probably, of the secondary carboxyl group of glutamic acid or of aspartic acid and a tyrosine phenol group in close proximity so that they can form hydrogen or hydrophobic bonds with the substrate in some unique manner that permits hydrolysis to occur at an accelerated rate. The Rockefeller University Press 1962-03-01 /pmc/articles/PMC2195218/ /pubmed/13906833 Text en Copyright © Copyright, 1962, by The Rockefeller Institute Press. 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. Pepsinogen and Pepsin |
title | Pepsinogen and Pepsin |
title_full | Pepsinogen and Pepsin |
title_fullStr | Pepsinogen and Pepsin |
title_full_unstemmed | Pepsinogen and Pepsin |
title_short | Pepsinogen and Pepsin |
title_sort | pepsinogen and pepsin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195218/ https://www.ncbi.nlm.nih.gov/pubmed/13906833 |
work_keys_str_mv | AT herriottrogerm pepsinogenandpepsin |