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Cited by 235

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

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Zwizinski, C., Wickner, W.·1980·Journal of Biological Chemistry

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 to be dependent on membrane fractions. We now describe a 6,000-fold purification of a leader peptidase from the membranes of uninfected Escherichia coli. This leader peptidase was assayed by its ability to cleave the 23-residue leader peptide from procoat, the precursor to bacteriophage M13 coat protein. Immunoprecipitation and amino acid sequencing showed that this enzyme cleaved procoat to produce authentic coat protein. No factors other than the leader peptidase were found to be required for the conversion of procoat protein to coat protein.

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Metadata

Authors
Zwizinski, C., & Wickner, W.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1980-08
Volume
255
Issue
16
Pages
7973-7977
ISSN
0021-9258 (ISSN-L)
OpenAlex
W175935117
Cited by
235
References
1
FWCI
18.44
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Purification and characterization of leader (signal) peptidase from Escherichia coli. https://app.cochat.ai/papers/10.1016/s0021-9258(19)43928-8
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Zwizinski, C., & Wickner, W. (1980). Purification and characterization of leader (signal) peptidase from Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)43928-8

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