Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: endoproteolytic cleavage of nascent f1 pre-coat protein.

@article{Chang1978DetectionOP,
  title={Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: endoproteolytic cleavage of nascent f1 pre-coat protein.},
  author={C N Chang and Gunter Blobel and Peter Model},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1978},
  volume={75 1},
  pages={361-5}
}
An inverted membrane vesicle fraction isolated from uninfected Escherichia coli and largely derived from the inner membrane has been shown to contain an endoproteolytic activity that cleaves nascent bacteriophage f1 pre-coat protein into two identifiable products. The electrophoretic mobility on sodium dodecyl sulfate/urea/polyacrylamide gels and the partial amino-terminal sequence of the larger fragment were indistinguishable from those of the mature phage coat protein. Partial amino-terminal… CONTINUE READING