Alpha synuclein is an abundant neurological protein that has been implicated in a number of neurodegenerative diseases. It has been proposed that the mechanism by which this protein elicits its effects in these diseases is through metal-protein interaction causing conformational changes which results in aggregation and oxidative stress. However the exact pathological role of alpha synuclein is yet to be elucidated and the interactions between it and metals have only been shown using recombinant proteins. Most recombinant protein techniques lack the machinery for incorporating post-translational modifications common to eukaryotic proteins, including chaperones for delivering copper. To investigate the metal status of native alpha synuclein we have purified it from both human erythrocytes and human brain tissue using non-denaturing techniques. Using size exclusion chromatography coupled to inductively coupled plasma – mass spectrometry we were able to directly determine the metal status of alpha-synuclein. Results indicated that alpha synuclein does not bind significant amounts of copper, iron or zinc, even when these metals were added to the protein in excess. In addition to this we used intact mass spectrometry to identify alpha synuclein, which was present in different truncated forms in the blood and the brain. Based on these results native alpha synuclein purified using these techniques is not a metalloprotein and can is present in multiple truncated versions in the blood and brain.