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. Author manuscript; available in PMC: 2013 Jun 27.
Published in final edited form as: J Am Chem Soc. 2012 Jun 13;134(25):10458–10468. doi: 10.1021/ja301221s

Fig 2. Isotope dependence of EPR spectra for 1:1 65Cu(II)-HM complex and the formation of dimeric species.

Fig 2

(a) Comparison of 14N- (red) and 15N- (blue) substituted ScoHM at 1:1 Cu:P. (b) and (c) Low-field hyperfine line expanded to reveal superhyperfine structure for 14N- and 15N-substituted proteins respectively. EPR instrumental settings were as listed in the legend to Figure 1. (d) Western blots of ATP7A membranes separated on blue native gels showing the presence of oligomeric forms of ATP7A. ATP7B treated in the same fashion is shown as a control. The following soluble proteins were used as molecular weight markers: 1048 kDa, IgM Pentamer; 720 kDa, Apoferritin Band 1; 480 kDa, Apoferritin Band 2; 242 kDa, B-phycoerythrin; 146 kDa, Lactate Dehydrogenase; 66 kDa, Bovine Serum Albumin.