A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
J. Clin. Invest. Isla Ogilvie, et al. 115:2784 doi:10.1172/JCI26020 [Go to this article.]

Figure 7
Immunoprecipitation of B17.2L and a subset of complex I subunits from normal human heart mitochondria. Mitochondria were isolated from normal human heart and immunoprecipitated with an immobilized anti-B17.2L antibody. (A) The immunoprecipitate was probed for the presence of B17.2L and the specific complex I subunits indicated to the right of the gels. COX-1, a subunit of complex IV, and SD70, a subunit of complex II, were used to control for nonspecific interactions. Lane I shows a sample of the mitochondrial protein applied to the immobilized antibody. Lane E represents half of the sample obtained following elution of the protein that specifically bound to the immobilized antibody. Lane W shows a sample of the final wash in the same volume as the eluate. (B) Quantitative analysis of the proteins immunoprecipitated by the anti-B17.2L antibody as obtained by densitometric analysis of the immunoblots.