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Life science application utilizing radiocarbon tracing
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Applied Nuclear Physics.
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Radiology, Oncology and Radiation Science, Section of Nuclear Medicine and PET.
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2013 (English)In: Radiocarbon, ISSN 0033-8222, E-ISSN 1945-5755, Vol. 55, no 2-3, 865-873 p.Article in journal (Refereed) Published
Abstract [en]

Radiocarbon-based accelerator mass spectrometry (AMS) facilities at Uppsala University include a measurement center for archaeological applications and a separate entity dedicated to life science research. This paper addresses the latter, with the intention of giving a brief description of the biomedical activities at our laboratory, as well as presenting new data. The ultra-small sample preparation method, which can be used down to a few µg C samples, is outlined and complemented with new results. Furthermore, it is shown that the average secondary ion current performance for small samples can be improved by increasing the distance between the cathode surface and the pressed graphite surface. Finally, data is presented for a new application: Amyloidoses are a group of diseases where the conformational changes in specific proteins’ structure lead to the formation of extracellular deposits that spread and increase in mass and eventually may lead to total organ failure and death. The formation timeframe is unknown and yet it is an important clue for the elucidation of the mechanism. We present results on bomb-peak dating of 4 different types of purified amyloid proteins from human postmortem heart and spleen samples. The data indicates that the average measured age of the carbon originating from the systemic amyloid types studied here correspond to a few years before the death of the subject. This suggests that a major part of the fibril formation takes place during the last few years before death, rather than as an accumulation of amyloid deposits over decades.

Place, publisher, year, edition, pages
2013. Vol. 55, no 2-3, 865-873 p.
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Physical Sciences
Research subject
Physics
Identifiers
URN: urn:nbn:se:uu:diva-207747DOI: 10.2458/azu_js_rc.55.16479OAI: oai:DiVA.org:uu-207747DiVA: diva2:855565
Available from: 2015-09-21 Created: 2013-09-18 Last updated: 2017-12-04Bibliographically approved

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Salehpour, MehranHåkansson, KarlWestermark, PerAntoni, GunnarWikström, GerhardPossnert, Göran

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Salehpour, MehranHåkansson, KarlWestermark, PerAntoni, GunnarWikström, GerhardPossnert, Göran
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Applied Nuclear PhysicsDepartment of Physics and AstronomyDepartment of Immunology, Genetics and PathologySection of Nuclear Medicine and PETCardiology
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