Abstract
Anti-idiotypic antibodies, prepared using a chemically synthesized signal peptide of a mitochondrial precursor protein, recognized a mitochondrial integral membrane protein (p32). Fab fragments derived from both anti-idiotypic antibodies and monospecific antibodies against purified p32 inhibited protein import into mitochondria. Moreover, anti-p32 antibodies specifically immunoprecipitated a precursor–p32 complex after detergent solubilization of mitochondria. Immunoelectron microscopy and subfractionation of mitochondria indicate that p32 is located in contact sites between the outer and inner mitochondrial membranes.
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Pain, D., Murakami, H. & Blobel, G. Identification of a receptor for protein import into mitochondria. Nature 347, 444–449 (1990). https://doi.org/10.1038/347444a0
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DOI: https://doi.org/10.1038/347444a0
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