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- W1645743076 abstract "The principle of the in vitro reconstitution of peroxisomal protein assembly is simple: newly synthesized peroxisomal proteins (labeled with [35S]methionine) are mixed with purified peroxisomes and the proteins enter the organelle in a time- and temperature-dependent fashion. Import is analyzed by digesting the nonimported proteins with a protease. Those proteins that have been imported into the peroxisomes are protected from proteolysis by the membrane of the organelle. This in vitro reconstitution of import requires a good supply of stable, purified peroxisomes, sufficient synthesis of radiolabeled peroxisomal proteins, appropriate incubation conditions for import, the selection of protease(s) that can digest nonimported proteins without destroying the organelle membrane, and careful controls. Each of these issues is discussed in detail in the chapter. To adapt the import assays for the study of another peroxisomal protein, it is necessary to verify that the protease protection assay functions for the new protein, and, if not, to find suitable conditions. The selection of the protease is based on two criteria: (1) the 35S-labeled protein has to be digestible by the protease and (2) the peroxisomes have to remain intact during the protease treatment." @default.
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- W1645743076 date "1991-01-01" @default.
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- W1645743076 title "Chapter 14 Protein Import into Peroxisomes in Vitro" @default.
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- W1645743076 doi "https://doi.org/10.1016/s0091-679x(08)61687-8" @default.
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