COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI
A comparison has been made of the relative velocity of hydrolysis of the various peptid linkings of the gelatin molecule when hydrolyzed by acid, alkali, pepsin or trypsin. It has been found that: 1. Those linkages which are most rapidly split by pepsin or trypsin are among the more resistant to ac...
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| Format: | Online |
| Language: | English |
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The Rockefeller University Press
1921
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140434/ |
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pubmed-2140434 |
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oai_dc |
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pubmed-21404342008-04-23 COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI Northrop, John H. Article A comparison has been made of the relative velocity of hydrolysis of the various peptid linkings of the gelatin molecule when hydrolyzed by acid, alkali, pepsin or trypsin. It has been found that: 1. Those linkages which are most rapidly split by pepsin or trypsin are among the more resistant to acid hydrolysis. 2. Those linkages which are hydrolyzed by pepsin are also hydrolyzed by trypsin. 3. Trypsin hydrolyzes linkages which are not attacked by pepsin. 4. Of the linkages which are hydrolyzed by both enzymes, those which are most rapidly hydrolyzed by pepsin are only slowly attacked by trypsin. 5. Those linkages which are attacked by trypsin or pepsin are among the ones first (most rapidly) hydrolyzed by alkali. In general it may be said that the course of the early stages of hydrolysis of gelatin is similar with alkali, trypsin, or pepsin and quite different with acid. The Rockefeller University Press 1921-09-20 /pmc/articles/PMC2140434/ /pubmed/19871916 Text en Copyright © Copyright, 1921, 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 |
Northrop, John H. |
| spellingShingle |
Northrop, John H. COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI |
| author_facet |
Northrop, John H. |
| author_sort |
Northrop, John H. |
| title |
COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI |
| title_short |
COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI |
| title_full |
COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI |
| title_fullStr |
COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI |
| title_full_unstemmed |
COMPARATIVE HYDROLYSIS OF GELATIN BY PEPSIN, TRYPSIN, ACID, AND ALKALI |
| title_sort |
comparative hydrolysis of gelatin by pepsin, trypsin, acid, and alkali |
| description |
A comparison has been made of the relative velocity of hydrolysis of the various peptid linkings of the gelatin molecule when hydrolyzed by acid, alkali, pepsin or trypsin. It has been found that: 1. Those linkages which are most rapidly split by pepsin or trypsin are among the more resistant to acid hydrolysis. 2. Those linkages which are hydrolyzed by pepsin are also hydrolyzed by trypsin. 3. Trypsin hydrolyzes linkages which are not attacked by pepsin. 4. Of the linkages which are hydrolyzed by both enzymes, those which are most rapidly hydrolyzed by pepsin are only slowly attacked by trypsin. 5. Those linkages which are attacked by trypsin or pepsin are among the ones first (most rapidly) hydrolyzed by alkali. In general it may be said that the course of the early stages of hydrolysis of gelatin is similar with alkali, trypsin, or pepsin and quite different with acid. |
| publisher |
The Rockefeller University Press |
| publishDate |
1921 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140434/ |
| _version_ |
1611422217601548288 |