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Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research

A marked difference in spin relaxation behavior due to hemoglobin magnetism was found for positive muons (μ(+)) in deoxyhemoglobin in comparison with that observed in oxyhemoglobin in aqueous solution at room temperature under zero and external longitudinal magnetic fields upto 0.4 Tesla. At the sam...

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Autores principales: Nagamine, Kanetada, Shimomura, Koichiro, Miyadera, Haruo, Kim, Yong-Jae, Scheicher, Ralph Hendrik, Das, Tara Prasad, Schultz, Jerome Samson
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japan Academy 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3756736/
https://www.ncbi.nlm.nih.gov/pubmed/24019590
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author Nagamine, Kanetada
Shimomura, Koichiro
Miyadera, Haruo
Kim, Yong-Jae
Scheicher, Ralph Hendrik
Das, Tara Prasad
Schultz, Jerome Samson
author_facet Nagamine, Kanetada
Shimomura, Koichiro
Miyadera, Haruo
Kim, Yong-Jae
Scheicher, Ralph Hendrik
Das, Tara Prasad
Schultz, Jerome Samson
author_sort Nagamine, Kanetada
collection PubMed
description A marked difference in spin relaxation behavior due to hemoglobin magnetism was found for positive muons (μ(+)) in deoxyhemoglobin in comparison with that observed in oxyhemoglobin in aqueous solution at room temperature under zero and external longitudinal magnetic fields upto 0.4 Tesla. At the same time, small but significant unique relaxation pattern was observed in nonmagnetic oxyhemoglobin. Combined with our previous measurements on hemoglobin in human blood, application of this type of measurement to the studies of the level of oxygenation in various regions of the human brain is suggested.
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spelling pubmed-37567362013-09-09 Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research Nagamine, Kanetada Shimomura, Koichiro Miyadera, Haruo Kim, Yong-Jae Scheicher, Ralph Hendrik Das, Tara Prasad Schultz, Jerome Samson Proc Jpn Acad Ser B Phys Biol Sci Articles A marked difference in spin relaxation behavior due to hemoglobin magnetism was found for positive muons (μ(+)) in deoxyhemoglobin in comparison with that observed in oxyhemoglobin in aqueous solution at room temperature under zero and external longitudinal magnetic fields upto 0.4 Tesla. At the same time, small but significant unique relaxation pattern was observed in nonmagnetic oxyhemoglobin. Combined with our previous measurements on hemoglobin in human blood, application of this type of measurement to the studies of the level of oxygenation in various regions of the human brain is suggested. The Japan Academy 2007-05 /pmc/articles/PMC3756736/ /pubmed/24019590 Text en © 2007 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Nagamine, Kanetada
Shimomura, Koichiro
Miyadera, Haruo
Kim, Yong-Jae
Scheicher, Ralph Hendrik
Das, Tara Prasad
Schultz, Jerome Samson
Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research
title Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research
title_full Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research
title_fullStr Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research
title_full_unstemmed Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research
title_short Hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research
title_sort hemoglobin magnetism in aqueous solution probed by muon spin relaxation and future applications to brain research
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3756736/
https://www.ncbi.nlm.nih.gov/pubmed/24019590
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