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.
Original language | English (US) |
---|---|
Pages (from-to) | 444-449 |
Number of pages | 6 |
Journal | Nature |
Volume | 347 |
Issue number | 6292 |
DOIs | |
State | Published - 1990 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- General