QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE

The uptake of glutaraldehyde by human red blood cells has been measured as a function of time by a freezing point osmometer. The rate of attachment of glutaraldehyde to the cell proteins is high over the first hour, declining to zero over a period of a few days. The number of glutaraldehyde molecule...

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Detalles Bibliográficos
Autores principales: Morel, Francois M. M., Baker, Richard F., Wayland, Harold
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1971
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108233/
https://www.ncbi.nlm.nih.gov/pubmed/5545112
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author Morel, Francois M. M.
Baker, Richard F.
Wayland, Harold
author_facet Morel, Francois M. M.
Baker, Richard F.
Wayland, Harold
author_sort Morel, Francois M. M.
collection PubMed
description The uptake of glutaraldehyde by human red blood cells has been measured as a function of time by a freezing point osmometer. The rate of attachment of glutaraldehyde to the cell proteins is high over the first hour, declining to zero over a period of a few days. The number of glutaraldehyde molecules cross-linking with each hemoglobin molecule is of the order of 200, in reasonable agreement with the calculated number of attachment sites. The cell membrane is immediately highly permeable to glutaraldehyde. Selective permeability to ions is lost during fixation. Ionic equilibrium is obtained only after a few hours. An optimum fixation technique for shape preservation is suggested.
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spelling pubmed-21082332008-05-01 QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE Morel, Francois M. M. Baker, Richard F. Wayland, Harold J Cell Biol Article The uptake of glutaraldehyde by human red blood cells has been measured as a function of time by a freezing point osmometer. The rate of attachment of glutaraldehyde to the cell proteins is high over the first hour, declining to zero over a period of a few days. The number of glutaraldehyde molecules cross-linking with each hemoglobin molecule is of the order of 200, in reasonable agreement with the calculated number of attachment sites. The cell membrane is immediately highly permeable to glutaraldehyde. Selective permeability to ions is lost during fixation. Ionic equilibrium is obtained only after a few hours. An optimum fixation technique for shape preservation is suggested. The Rockefeller University Press 1971-01-01 /pmc/articles/PMC2108233/ /pubmed/5545112 Text en Copyright © 1970 by The Rockefeller University Press 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
Morel, Francois M. M.
Baker, Richard F.
Wayland, Harold
QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE
title QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE
title_full QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE
title_fullStr QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE
title_full_unstemmed QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE
title_short QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE
title_sort quantitation of human red blood cell fixation by glutaraldehyde
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108233/
https://www.ncbi.nlm.nih.gov/pubmed/5545112
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AT waylandharold quantitationofhumanredbloodcellfixationbyglutaraldehyde

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