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Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli.

Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. Research Abstract Details 

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  • Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. Abstract Text:

    t suzukiT Suzuki,s ichiharaS Ichihara,s mizushimaS Mizushima,

    A signal peptide, a processing product of the precursor of the lipoprotein in the cytoplasmic membrane of Escherichia coli, has been purified through extractions with butanol and ethyl ether and chromatographies with a Sephadex LH-60 column and Sep-pak C18. Analysis of the amino acid composition and sequencing of the N- and C-termini indicate that the signal peptide was intact, suggesting that the first step of the signal peptide catabolism in the cytoplasmic membrane is the cleavage of the intact signal peptide. During the purification, the signal peptide exhibited unique features, including strong interaction with phospholipids. The possible importance of such features in the process of protein translocation across membranes is discussed.

    Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. Publishing Authors By Initials

    t suzukiT Suzuki,s ichiharaS Ichihara,s mizushimaS Mizushima,

    For similar peptides: protein sorting signals research abstracts see: peptides: protein sorting signals research

    PUBMED ID PMID:

    MEDLINE DATE:

    Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 103

    Page Numbers: 470-3

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Mar

    YEAR: 1988

    Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. Keywords Mesh Terms:

    KEYWORDS: Protein Sorting Signals

    MESH TERMS: isolation & purification

    Chemical & Substance for Abstract: Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. Information

    Substance Name: Protein Sorting Signals

    Registry Number: 0

    Grant and Affiliation Information for Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli.

    AFFILIATION: Laboratory of Microbiology, School of Agriculture, Nagoya University, Aichi.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: J Biochem

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    Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli Related Publications

     

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