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. 2015 Jan 8;10:2. doi: 10.1186/1750-1326-10-2

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© Cuchillo-Ibañez et al.; licensee BioMed Central. 2015

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Characterization of APP complexes by native-PAGE and sucrose gradient ultracentrifugation. (A) APP complexes from the brain (frontal cortex from NDC subjects) and CSF samples (NDC subjects) were analyzed by blue native-PAGE. Incubation of blots with antibodies for the different APP epitopes confirmed the presence of APP dimers in brain extracts and CSF samples (~242 kDa), but also the existence of APP complexes with higher molecular weight. A CSF sample denatured by boiling at 95°C for 5 min under fully reducing conditions (Dn) was also analyzed by blue native-PAGE to warrant the migration of the monomeric sAPP band. (B) Brain extracts and CSF samples were also fractionated on 5-20% sucrose density gradients. The fractions (collected from the top of each tube) were immunoblotted for APP with the 6E10 antibody, and additionally with IBL-β and Sigma-Ct antibodies for CSF samples. Enzymes of known sedimentation coefficient, β-galactosidase (G, 16.0S; ~540 kDa), catalase (C, 11.4S; ~232 kDa) and alkaline phosphatase (P, 6.1S; ~140-160 kDa) were used as internal markers.