To obtain insight into the role of lipids in the translocation of extramitochondrially synthesized proteins, we studied the ability of apocytochrome c to pass lipid bilayers. With polyacrylamide gel electrophoresis, the digestion of externally added apocytochrome c by trypsin, enclosed in lipid vesicles, was followed. The experiments demonstrate that apocytochrome c is able to pass a lipid barrier and this process shows both a lipid- and protein specificity. The most probable molecular mechanisms involved in this phenomenon are discussed.
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