A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O

All enzyme that destroys DPN has been found in fractionated and highly concentrated streptococcal preparations that also contain streptolysin O. The enzyme—streptococcal DPNase—was shown by electrophoretic separation and by other means to be distinct from streptolysin O. It is non-dialyzable, heat-l...

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Detalles Bibliográficos
Autores principales: Carlson, Arthur S., Kellner, Aaron, Bernheimer, Alan W., Freeman, Elizabeth B.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1957
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136732/
https://www.ncbi.nlm.nih.gov/pubmed/13439111
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author Carlson, Arthur S.
Kellner, Aaron
Bernheimer, Alan W.
Freeman, Elizabeth B.
author_facet Carlson, Arthur S.
Kellner, Aaron
Bernheimer, Alan W.
Freeman, Elizabeth B.
author_sort Carlson, Arthur S.
collection PubMed
description All enzyme that destroys DPN has been found in fractionated and highly concentrated streptococcal preparations that also contain streptolysin O. The enzyme—streptococcal DPNase—was shown by electrophoretic separation and by other means to be distinct from streptolysin O. It is non-dialyzable, heat-labile, and has optimal activity in the pH range 7.2 to 7.8. The enzyme has a high degree of specificity for DPN, which it splits at the nicotinamide-ribose linkage.
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spelling pubmed-21367322008-04-17 A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O Carlson, Arthur S. Kellner, Aaron Bernheimer, Alan W. Freeman, Elizabeth B. J Exp Med Article All enzyme that destroys DPN has been found in fractionated and highly concentrated streptococcal preparations that also contain streptolysin O. The enzyme—streptococcal DPNase—was shown by electrophoretic separation and by other means to be distinct from streptolysin O. It is non-dialyzable, heat-labile, and has optimal activity in the pH range 7.2 to 7.8. The enzyme has a high degree of specificity for DPN, which it splits at the nicotinamide-ribose linkage. The Rockefeller University Press 1957-07-01 /pmc/articles/PMC2136732/ /pubmed/13439111 Text en Copyright © Copyright, 1957, by The Rockefeller Institute for Medical Research New York 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
Carlson, Arthur S.
Kellner, Aaron
Bernheimer, Alan W.
Freeman, Elizabeth B.
A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O
title A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O
title_full A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O
title_fullStr A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O
title_full_unstemmed A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O
title_short A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O
title_sort streptococcal enzyme that acts specifically upon diphosphopyridine nucleotide: characterization of the enzyme and its separation from streptolysin o
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136732/
https://www.ncbi.nlm.nih.gov/pubmed/13439111
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