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Life Science Applications Utilizing Radiocarbon Tracing

Published online by Cambridge University Press:  09 February 2016

M Salehpour*
Affiliation:
Department of Physics and Astronomy, Applied Nuclear Physics Division, Ion Physics, PO Box 516, SE-751 20 Uppsala, Sweden
K Håkansson
Affiliation:
Department of Physics and Astronomy, Applied Nuclear Physics Division, Ion Physics, PO Box 516, SE-751 20 Uppsala, Sweden
P Westermark
Affiliation:
Department of Immunology, Genetics and Pathology, Molecular and Morphological Pathology, Rudbeck Laboratory, Uppsala University, SE-751 85 Uppsala, Sweden
G Antoni
Affiliation:
PET-Centre, Centre for Medical Imaging, Uppsala University Hospital, SE-751 85 Uppsala, Sweden
G Wikström
Affiliation:
Department of Medical Sciences, Cardiology, Uppsala University Hospital, SE-751 85 Uppsala, Sweden
G Possnert
Affiliation:
Department of Physics and Astronomy, Applied Nuclear Physics Division, Ion Physics, PO Box 516, SE-751 20 Uppsala, Sweden
*
Corresponding author: mehran.salehpour@physics.uu.se.

Abstract

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.

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Copyright
Copyright © 2013 by the Arizona Board of Regents on behalf of the University of Arizona 

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