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THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE

1. Acid-inactivated yeast invertase could not be regenerated in the presence of the proteolytic enzymes trypsin, pepsin, and chymotrypsin. 2. Certain foreign proteins of non-enzymatic nature partially inhibited the reactivation of acid-inactivated invertase. 3. Certain proteins as gelatin, lacto-glo...

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Detalles Bibliográficos
Autores principales: Wagreich, Harry, Schwartz, Lawrence I., Kamin, Henry
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1941
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142033/
https://www.ncbi.nlm.nih.gov/pubmed/19873266
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author Wagreich, Harry
Schwartz, Lawrence I.
Kamin, Henry
author_facet Wagreich, Harry
Schwartz, Lawrence I.
Kamin, Henry
author_sort Wagreich, Harry
collection PubMed
description 1. Acid-inactivated yeast invertase could not be regenerated in the presence of the proteolytic enzymes trypsin, pepsin, and chymotrypsin. 2. Certain foreign proteins of non-enzymatic nature partially inhibited the reactivation of acid-inactivated invertase. 3. Certain proteins as gelatin, lacto-globulin, and carbohydrate-free horse crystalbumin did not prevent the reactivation of invertase at all. 4. Highly purified reactivated invertase was shown to exhibit an effect typical of original native invertase; that is, acceleration of its activity in presence of foreign protein at pH 3.0. 5. Native invertase was not digested by trypsin and chymotrypsin. 6. The addition of trypsin and chymotrypsin to reactivating invertase did not affect the invertase which had already reverted to the active form, but prevented further reactivation of inactive invertase.
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spelling pubmed-21420332008-04-23 THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE Wagreich, Harry Schwartz, Lawrence I. Kamin, Henry J Gen Physiol Article 1. Acid-inactivated yeast invertase could not be regenerated in the presence of the proteolytic enzymes trypsin, pepsin, and chymotrypsin. 2. Certain foreign proteins of non-enzymatic nature partially inhibited the reactivation of acid-inactivated invertase. 3. Certain proteins as gelatin, lacto-globulin, and carbohydrate-free horse crystalbumin did not prevent the reactivation of invertase at all. 4. Highly purified reactivated invertase was shown to exhibit an effect typical of original native invertase; that is, acceleration of its activity in presence of foreign protein at pH 3.0. 5. Native invertase was not digested by trypsin and chymotrypsin. 6. The addition of trypsin and chymotrypsin to reactivating invertase did not affect the invertase which had already reverted to the active form, but prevented further reactivation of inactive invertase. The Rockefeller University Press 1941-11-20 /pmc/articles/PMC2142033/ /pubmed/19873266 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
Wagreich, Harry
Schwartz, Lawrence I.
Kamin, Henry
THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE
title THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE
title_full THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE
title_fullStr THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE
title_full_unstemmed THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE
title_short THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE
title_sort influence of proteins on the reactivation of yeast invertase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142033/
https://www.ncbi.nlm.nih.gov/pubmed/19873266
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