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  • 1
    Electronic Resource
    Electronic Resource
    Voltage-sensitive ion channel ofEscherichia coli (1989)
    Springer
    The journal of membrane biology 112 (1989), S. 267-275 
    Details
    ISSN: 1432-1424
    Keywords: Escherichia coli ; outer membrane ; ion channel ; patch clamp ; porin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A voltage-sensitive, cation-selective ion channel ofEscherichia coli has been reconstituted into liposomes and studied with the patch-clamp method. The single channel conductance was 91 pS in symmetric solutions of 150mm KCl. Many channels were open most of the time, with frequent brief transitions to closed levels. Multiple conducting units could close and reopen simultaneously, and this apparent cooperativity in gating was increases with depolarizing voltages. Above a voltage threshold, the channels closed irreversibly, often in groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870957
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  • 2
    Electronic Resource
    Electronic Resource
    A single amino acid substitution alters conductance and gating of OmpC porin ofEscherichia coli (1991)
    Springer
    The journal of membrane biology 119 (1991), S. 267-275 
    Details
    ISSN: 1432-1424
    Keywords: Escherichia coli ; ion channel ; mutant ; patch clamp ; porin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We have reconstituted into liposomes outer-membrane fractions fromEscherichia coil strains which express OmpC porins with altered pore properties. Single-channel experiments were performed with the patch-clamp technique on blisters generated from the reconstituted liposomes. Our goal was to identify positively the activity pattern of OmpC in our reconstituted system. The properties of the parent strain were compared to those of a strain whose OmpC porin has a single amino acid substitution in a postulated transmembrane segment. The parent and the mutant strain each exhibit a cation-selective channel of high open probability and gating to closed levels of various amplitudes. However, the mutant channel appeared to be 9 to 30% larger in unit conductance. It tended to close and reopen most often in groups of three units, as opposed to two units in the parent channel. The results are discussed in terms of the observed phenotype and of their implication as to the structure-function relationship of the porin channels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868731
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