Purification and characterization of leader (signal) peptidase from Escherichia coli.

Abstract

Many membrane proteins and secreted proteins are synthesized in precursor form with 15 to 30 additional NH2-terminal residues. These "leader peptides" (pre-pieces, signal peptides) are removed as these proteins cross or insert into cellular membranes. "Leader peptidase" activities which catalyze this cleavage have been detected in crude extracts and found… (More)

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Cite this paper

@article{Zwizinski1980PurificationAC, title={Purification and characterization of leader (signal) peptidase from Escherichia coli.}, author={Craig W Zwizinski and William Wickner}, journal={The Journal of biological chemistry}, year={1980}, volume={255 16}, pages={7973-7} }