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Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes
We measured the rate of oxygen transport through thin (165 µ) films of packed erythrocytes (Hb concentration = 30 g/100 ml). Under optimal conditions steady-state O(2) diffusion was nearly three times that found when the hemoglobin was prevented from acting as a carrier molecule by carbon monoxide b...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1969
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2202888/ https://www.ncbi.nlm.nih.gov/pubmed/5769422 |
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author | Kutchai, Howard Staub, Norman C. |
author_facet | Kutchai, Howard Staub, Norman C. |
author_sort | Kutchai, Howard |
collection | PubMed |
description | We measured the rate of oxygen transport through thin (165 µ) films of packed erythrocytes (Hb concentration = 30 g/100 ml). Under optimal conditions steady-state O(2) diffusion was nearly three times that found when the hemoglobin was prevented from acting as a carrier molecule by carbon monoxide binding or high oxygen back pressure. After each experiment we measured hemolysis and found that it averaged less than 1%. Hemolysis could not account for the facilitation, thus proving that facilitated transport of O(2) by hemoglobin can occur in red blood cells. The rate of facilitated transport was identical for Hb solutions of equal concentration to the cells. We interpret this to mean that under the conditions of our experiments the red cell membrane offers no detectable diffusion resistance to O(2) and that the mobility of Hb in intact red cells is the same as in concentrated Hb solution. |
format | Text |
id | pubmed-2202888 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1969 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22028882008-04-23 Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes Kutchai, Howard Staub, Norman C. J Gen Physiol Article We measured the rate of oxygen transport through thin (165 µ) films of packed erythrocytes (Hb concentration = 30 g/100 ml). Under optimal conditions steady-state O(2) diffusion was nearly three times that found when the hemoglobin was prevented from acting as a carrier molecule by carbon monoxide binding or high oxygen back pressure. After each experiment we measured hemolysis and found that it averaged less than 1%. Hemolysis could not account for the facilitation, thus proving that facilitated transport of O(2) by hemoglobin can occur in red blood cells. The rate of facilitated transport was identical for Hb solutions of equal concentration to the cells. We interpret this to mean that under the conditions of our experiments the red cell membrane offers no detectable diffusion resistance to O(2) and that the mobility of Hb in intact red cells is the same as in concentrated Hb solution. The Rockefeller University Press 1969-05-01 /pmc/articles/PMC2202888/ /pubmed/5769422 Text en Copyright © 1969 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 Kutchai, Howard Staub, Norman C. Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes |
title | Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes |
title_full | Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes |
title_fullStr | Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes |
title_full_unstemmed | Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes |
title_short | Steady-State, Hemoglobin-Facilitated O(2) Transport in Human Erythrocytes |
title_sort | steady-state, hemoglobin-facilitated o(2) transport in human erythrocytes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2202888/ https://www.ncbi.nlm.nih.gov/pubmed/5769422 |
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