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ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN

It has been shown by the work presented in this paper that it is possible to carry out a stepwise dephosphorylation of ovalbumin. With the aid of a prostate phosphatase that attacks only one of the two phosphorus-containing groups in the major component, A(1), of ovalbumin, a protein, A(2), containi...

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Autor principal: Perlmann, Gertrude E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1952
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147319/
https://www.ncbi.nlm.nih.gov/pubmed/14955615
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author Perlmann, Gertrude E.
author_facet Perlmann, Gertrude E.
author_sort Perlmann, Gertrude E.
collection PubMed
description It has been shown by the work presented in this paper that it is possible to carry out a stepwise dephosphorylation of ovalbumin. With the aid of a prostate phosphatase that attacks only one of the two phosphorus-containing groups in the major component, A(1), of ovalbumin, a protein, A(2), containing 1 atom of phosphorus per mole has been prepared. Further dephosphorylation with an enzyme of intestinal origin gives a phosphorus-free ovalbumin, A(3). Plakalbumin has been similarly dephosphorylated to give P(2) and P(3). Significant changes in the electrophoretic mobility accompany each dephosphorylation step. This, together with the phosphorus content of the proteins and the crystal form, has been used to characterize and study the five modifications of ovalbumin thus produced.
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spelling pubmed-21473192008-04-23 ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN Perlmann, Gertrude E. J Gen Physiol Article It has been shown by the work presented in this paper that it is possible to carry out a stepwise dephosphorylation of ovalbumin. With the aid of a prostate phosphatase that attacks only one of the two phosphorus-containing groups in the major component, A(1), of ovalbumin, a protein, A(2), containing 1 atom of phosphorus per mole has been prepared. Further dephosphorylation with an enzyme of intestinal origin gives a phosphorus-free ovalbumin, A(3). Plakalbumin has been similarly dephosphorylated to give P(2) and P(3). Significant changes in the electrophoretic mobility accompany each dephosphorylation step. This, together with the phosphorus content of the proteins and the crystal form, has been used to characterize and study the five modifications of ovalbumin thus produced. The Rockefeller University Press 1952-05-20 /pmc/articles/PMC2147319/ /pubmed/14955615 Text en Copyright © Copyright, 1952, 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
Perlmann, Gertrude E.
ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN
title ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN
title_full ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN
title_fullStr ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN
title_full_unstemmed ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN
title_short ENZYMATIC DEPHOSPHORYLATION OF OVALBUMIN AND PLAKALBUMIN
title_sort enzymatic dephosphorylation of ovalbumin and plakalbumin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147319/
https://www.ncbi.nlm.nih.gov/pubmed/14955615
work_keys_str_mv AT perlmanngertrudee enzymaticdephosphorylationofovalbuminandplakalbumin