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. 2009 Apr 17;284(16):10855–10867. doi: 10.1074/jbc.M804813200

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Copyright © 2009, The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 8. — Alteration of cp-2 cleavage site changes biochemical properties of Htt protein. A, the procedure used to fractionate and dissociate Htt proteins (see “Experimental Procedures”). B, Western blots of subcellular fractions from HEK293 cells transfected with the indicated constructs: 1, native PAGE of soluble cytoplasmic fractions; 2, SDS-PAGE of soluble cytoplasmic fractions; 3, SDS-PAGE of the pellet, with SDS-insoluble material detected on top of the gel; 4, SDS-PAGE of formic acid-soluble aggregate fractions. Htt fragments were detected with antibodies to exon 1. ^*, minimal immunoreactivity is observed for Htt-N511-52Q-Δ167-170 following formic acid treatment. ^**, less SDS-insoluble material is detected for the Δ167-170 mutant than for unaltered N511-52Q. ^***, new high molecular weight soluble complexes are detected for Htt-N511-52Q-Δ167-170 in native conditions.