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. 2018 Jan 17;293(12):4244–4261. doi: 10.1074/jbc.RA118.001777

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© 2018 Lloyd-Lewis et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

Author's Choice—Final version free via Creative Commons CC-BY license.

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Figure 2. — Membrane fractionation of isolated EpH4 lysosomes. A, hypotonic lysis of lysosomes isolated from EpH4 cells using iron nanoparticles to separate the LM from the LC. LAMP2 immunoblotting shows its enrichment in the LM fraction. Ctsl, cathepsin L (sc, single chain: dc, double chain); SN, post-magnetic supernatant. B, cathepsin activity in EpH4 lysosomes isolated using iron nanoparticles and extracted using TX-100 (TX+, total lysosomal content) or by hypotonic lysis and fractionation (LM+, membrane fractions; LC+, matrix) compared with unlabeled control samples (TX−, LM−, and LC−). C and D, freeze-thawing of lysosomes improved lysosome membrane separation from the lysosomal matrix. Cathepsin (C) and β-glucuronidase activity (D) in the LC fraction is shown as -fold of LM. AFU, arbitrary fluorescence units.