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A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN

1. The retarding effect of plasma on the action of trypsin can be measured quantitatively. 2. The nature of the reaction involved in effecting the retardation has been subjected to an experimental study. 3. Evidence is presented which indicates that the equilibrium between the inhibitive agent and t...

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Autores principales: Hussey, Raymond G., Northrop, John H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1923
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140533/
https://www.ncbi.nlm.nih.gov/pubmed/19872000
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author Hussey, Raymond G.
Northrop, John H.
author_facet Hussey, Raymond G.
Northrop, John H.
author_sort Hussey, Raymond G.
collection PubMed
description 1. The retarding effect of plasma on the action of trypsin can be measured quantitatively. 2. The nature of the reaction involved in effecting the retardation has been subjected to an experimental study. 3. Evidence is presented which indicates that the equilibrium between the inhibitive agent and trypsin is reached practically instantaneously and is rapidly and completely reversible. 4. This equilibrium has been studied by experiments in which we have observed (1) the effect of adding increasing amounts of plasma to a constant amount of trypsin, (2) the effect of varying the amount of trypsin while the plasma was constant, (3) the effect of dilution on the trypsin-plasma mixture. 5. The results of these experiments are discussed and it is stated that they are in quantitative agreement with the law of mass action. 6. An equation was found which fits the curves for the experiments mentioned in (4). This equation was developed from the assumption that 1 molecule of trypsin combined with 1 molecule of inhibitor to form 1 molecule of trypsin-inhibitor compound. The agreement between the results calculated by this equation and the observed results is satisfactory. It is pointed out that the equation contains two arbitrary constants and the bearing this fact may have on the calculated results is discussed. 7. We conclude from the results of our study that we have adduced evidence which suggests the following statement regarding the so called "antitryptic" property of blood. The inhibitive agent and trypsin combine to form an inactive but dissociable compound. The reaction in equilibrium is expressed by the equation Trypsin + inhibitor ⇌ trypsin-inhibitor The conditions of equilibrium are apparently governed by the law of mass action. The behavior of the equilibrium is therefore similar to the behavior of other equilibria between different inhibitive agents and enzymes discussed in the paper.
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spelling pubmed-21405332008-04-23 A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN Hussey, Raymond G. Northrop, John H. J Gen Physiol Article 1. The retarding effect of plasma on the action of trypsin can be measured quantitatively. 2. The nature of the reaction involved in effecting the retardation has been subjected to an experimental study. 3. Evidence is presented which indicates that the equilibrium between the inhibitive agent and trypsin is reached practically instantaneously and is rapidly and completely reversible. 4. This equilibrium has been studied by experiments in which we have observed (1) the effect of adding increasing amounts of plasma to a constant amount of trypsin, (2) the effect of varying the amount of trypsin while the plasma was constant, (3) the effect of dilution on the trypsin-plasma mixture. 5. The results of these experiments are discussed and it is stated that they are in quantitative agreement with the law of mass action. 6. An equation was found which fits the curves for the experiments mentioned in (4). This equation was developed from the assumption that 1 molecule of trypsin combined with 1 molecule of inhibitor to form 1 molecule of trypsin-inhibitor compound. The agreement between the results calculated by this equation and the observed results is satisfactory. It is pointed out that the equation contains two arbitrary constants and the bearing this fact may have on the calculated results is discussed. 7. We conclude from the results of our study that we have adduced evidence which suggests the following statement regarding the so called "antitryptic" property of blood. The inhibitive agent and trypsin combine to form an inactive but dissociable compound. The reaction in equilibrium is expressed by the equation Trypsin + inhibitor ⇌ trypsin-inhibitor The conditions of equilibrium are apparently governed by the law of mass action. The behavior of the equilibrium is therefore similar to the behavior of other equilibria between different inhibitive agents and enzymes discussed in the paper. The Rockefeller University Press 1923-01-20 /pmc/articles/PMC2140533/ /pubmed/19872000 Text en Copyright © Copyright, 1923, 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
Hussey, Raymond G.
Northrop, John H.
A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN
title A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN
title_full A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN
title_fullStr A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN
title_full_unstemmed A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN
title_short A STUDY OF THE EQUILIBRIUM BETWEEN THE SO CALLED "ANTITRYPSIN" OF THE BLOOD AND TRYPSIN
title_sort study of the equilibrium between the so called "antitrypsin" of the blood and trypsin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140533/
https://www.ncbi.nlm.nih.gov/pubmed/19872000
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