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Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , <t>Smac/DIABLO,</t> Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.
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Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , <t>Smac/DIABLO,</t> Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.
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Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , <t>Smac/DIABLO,</t> Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.
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Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , <t>Smac/DIABLO,</t> Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.
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Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , <t>Smac/DIABLO,</t> Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.
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Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , <t>Smac/DIABLO,</t> Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.
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Santa Cruz Biotechnology rabbit polyclonal anti smac
Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , <t>Smac/DIABLO,</t> Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.
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Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , Smac/DIABLO, Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.

Journal: PLoS ONE

Article Title: Destabilization of the Outer and Inner Mitochondrial Membranes by Core and Linker Histones

doi: 10.1371/journal.pone.0035357

Figure Lengend Snippet: Mitochondria were incubated as described in the legend of , whereupon they were sedimented by centrifugation and proteins of the resulting pellets ( P ) and supernatants ( S ) were analyzed by immunoblotting. Panel A : release of cytochrome c , Smac/DIABLO, Omi/HtrA2, AIF, endonuclease G, and LACTB by histones, tBID and p53. The concentrations used were: 5 µM histone H1.2; 10 µM histone H2A, 10 µM histone H2B, 5 µM histone H3, 5 µM histone H4, 1 µM tBID, and 1 µM p53. Panel B : effect of cyclosporin A on the histone-induced release of cytochrome c and Smac/DIABLO. Panel C : accessibility of AIF and LACTB to trypsin hydrolysis in the presence of histones.

Article Snippet: Polyclonal anti-histone H1 antibody, polyclonal anti-histone H2A antibody, and polyclonal anti-histone H2B antibody were from Santa-Cruz Biotechology, polyclonal anti-histone H3 antibody was from Cell Signaling Technology, polyclonal anti-histone H4 antibody, monoclonal anti-cytochrome c antibody, and polyclonal anti-AIF antibody were from Millipore, polyclonal anti-endonuclease G antibody was from Serotec, polyclonal anti-HtrA2/Omi antibody was from Alexis Biochemicals, polyclonal anti-Smac/DIABLO antibody was from Stressgen, polyclonal anti-LACTB antibody was prepared as previously described , anti-rabbit IgG peroxidase conjugate and anti-mouse IgG peroxidase conjugate were from Sigma, and anti-rabbit IgG Alexa 488 conjugate was from Invitrogen.

Techniques: Incubation, Centrifugation, Western Blot