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THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE
1. Some 16 amino acids (not containing SH or S-S groups) did not affect the reactivation of yeast invertase inactivated by acid. 2. Cysteine, reduced glutathione, homocysteine, thiophenol, and thioglycollic acid accelerated the reactivation of yeast invertase. 3. Cystine, oxidized glutathione, and h...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1943
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142567/ https://www.ncbi.nlm.nih.gov/pubmed/19873360 |
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author | Wagreich, Harry Halpert, Wesley Hirschman, Albert |
author_facet | Wagreich, Harry Halpert, Wesley Hirschman, Albert |
author_sort | Wagreich, Harry |
collection | PubMed |
description | 1. Some 16 amino acids (not containing SH or S-S groups) did not affect the reactivation of yeast invertase inactivated by acid. 2. Cysteine, reduced glutathione, homocysteine, thiophenol, and thioglycollic acid accelerated the reactivation of yeast invertase. 3. Cystine, oxidized glutathione, and homocystine inhibited the reactivation of yeast invertase. 4. The compounds mentioned in 2 and 3 did not affect native invertase. 5. The use of compounds in which the H of the SH group of homocysteine was substituted by a methyl or benzyl nullified the accelerative effect. 6. The longer the cysteine remained in contact with the inactivating enzyme, the greater was the velocity of the reactivated invertase. 7. The per cent acceleration by cysteine is inversely proportional to the control rate. |
format | Text |
id | pubmed-2142567 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1943 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21425672008-04-23 THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE Wagreich, Harry Halpert, Wesley Hirschman, Albert J Gen Physiol Article 1. Some 16 amino acids (not containing SH or S-S groups) did not affect the reactivation of yeast invertase inactivated by acid. 2. Cysteine, reduced glutathione, homocysteine, thiophenol, and thioglycollic acid accelerated the reactivation of yeast invertase. 3. Cystine, oxidized glutathione, and homocystine inhibited the reactivation of yeast invertase. 4. The compounds mentioned in 2 and 3 did not affect native invertase. 5. The use of compounds in which the H of the SH group of homocysteine was substituted by a methyl or benzyl nullified the accelerative effect. 6. The longer the cysteine remained in contact with the inactivating enzyme, the greater was the velocity of the reactivated invertase. 7. The per cent acceleration by cysteine is inversely proportional to the control rate. The Rockefeller University Press 1943-05-20 /pmc/articles/PMC2142567/ /pubmed/19873360 Text en Copyright © Copyright, 1943, 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 Wagreich, Harry Halpert, Wesley Hirschman, Albert THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE |
title | THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE |
title_full | THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE |
title_fullStr | THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE |
title_full_unstemmed | THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE |
title_short | THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE |
title_sort | influence of amino acids on the reactivation of yeast invertase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142567/ https://www.ncbi.nlm.nih.gov/pubmed/19873360 |
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