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A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method

In one of the current histochemical methods for dehydrogenases and diaphorases the final product is a metal-formazan dye derived from reduction of an N-thiazolyl-substituted tetrazolium. Sites of enzymic activity consistently appear as intramitochondrial dots 0.2 to 0.3 µ in diameter. When applied t...

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Detalles Bibliográficos
Autores principales: Pearse, A. G. E., Scarpelli, D. G., Hess, R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1960
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224817/
https://www.ncbi.nlm.nih.gov/pubmed/14431240
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author Pearse, A. G. E.
Scarpelli, D. G.
Hess, R.
author_facet Pearse, A. G. E.
Scarpelli, D. G.
Hess, R.
author_sort Pearse, A. G. E.
collection PubMed
description In one of the current histochemical methods for dehydrogenases and diaphorases the final product is a metal-formazan dye derived from reduction of an N-thiazolyl-substituted tetrazolium. Sites of enzymic activity consistently appear as intramitochondrial dots 0.2 to 0.3 µ in diameter. When applied to active particles from disrupted mitochondria (Keilin-Hartree preparation, electron transport particle, Cooper-Lehninger particle) the individual particles appear as black dots 0.1 to 0.3 µ in diameter. It is clear that formazan is deposited progressively upon the particles and the results suggest that the latter may be spatially arranged in mitochondria so that areas of activity are separated by quiescent regions.
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spelling pubmed-22248172008-05-01 A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method Pearse, A. G. E. Scarpelli, D. G. Hess, R. J Biophys Biochem Cytol Article In one of the current histochemical methods for dehydrogenases and diaphorases the final product is a metal-formazan dye derived from reduction of an N-thiazolyl-substituted tetrazolium. Sites of enzymic activity consistently appear as intramitochondrial dots 0.2 to 0.3 µ in diameter. When applied to active particles from disrupted mitochondria (Keilin-Hartree preparation, electron transport particle, Cooper-Lehninger particle) the individual particles appear as black dots 0.1 to 0.3 µ in diameter. It is clear that formazan is deposited progressively upon the particles and the results suggest that the latter may be spatially arranged in mitochondria so that areas of activity are separated by quiescent regions. The Rockefeller University Press 1960-04-01 /pmc/articles/PMC2224817/ /pubmed/14431240 Text en Copyright © Copyright, 1960, by The Rockefeller Institute Press
spellingShingle Article
Pearse, A. G. E.
Scarpelli, D. G.
Hess, R.
A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method
title A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method
title_full A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method
title_fullStr A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method
title_full_unstemmed A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method
title_short A Cytochemical Study of the Dehydrogenases of Mitochondria and Mitochondrial Particulates by a Monotetrazolium-Cobalt Chelation Method
title_sort cytochemical study of the dehydrogenases of mitochondria and mitochondrial particulates by a monotetrazolium-cobalt chelation method
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224817/
https://www.ncbi.nlm.nih.gov/pubmed/14431240
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