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Antonenkov VD Rokka A Sormunen RT Benz R Hiltunen JK 《Cellular and molecular life sciences : CMLS》2005,62(23):2886-2895
Mouse liver peroxisomes were isolated by centrifugation in a self-generated Percoll gradient followed by an Optiprep density
gradient centrifugation. Peroxisomes contributed 90–96% of the total protein content in the fraction, as confirmed by marker
enzyme assays, protein pattern in SDS-PAGE, immunoblotting, and electron microscopy. Solubilized peroxisomal membrane proteins
were reconstituted into a planar lipid bilayer. A single-channel conductance monitoring of the reconstituted lipid bilayer
revealed the presence of two pore-forming components with a conductance in 1 M KCl of 1.3 nS and 2.5 nS. Control experiments
with fractions enriched in mitochondria, lysosomes, and fragments of endoplasmic reticulum showed that the peroxisomal channel-forming
activities were not due to admixture of isolated peroxisomes with other cellular organelles. The peroxisomal channels were
well preserved in membrane preparations but became unstable after solubilization from the membranes by detergent.
Received 27 May 2005; received after revision 23 September 2005; accepted 11 October 2005 相似文献
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