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  • 1
    ISSN: 1432-1912
    Keywords: Smooth muscle ; ATP ; Nicorandil ; K-channels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Nicorandil (10 μmol/l–0.3 mmol/l) and ATP (1 μmol/l–0.1 mmol/l) hyperpolarized the membrane of circular smooth muscle of the guinea-pig small intestine and increased conductance of the membrane probably to K ions as estimated by the effect on the current-voltage relationship. In the presence of a maximally hyperpolarizing concentration of nicorandil (0.1 mmol/l), ATP produced a further hyperpolarization of 5 mV. The ATP-induced but not the nicorandil-induced hyperpolarization required the presence of Ca in the medium, and the ATP-induced hyperpolarization was blocked by apamin treatment (1 nmol/l) or by MnCl2 (1.3 mmol/l). On the other hand, both hyperpolarization responses were blocked by the local anaesthetics procaine (0.1–1 mmol/l), lidocaine (0.1–1 mmol/l) or cocaine (0.3–1 mmol/l), with different potencies. Field stimulation of smooth muscle of the small intestine produced inhibitory junction potentials (i.j.p.s) and these were inhibited by apamin (10 nmol/l–100 nmol/l). In the presence of ATP, the amplitude of the i.j.p.s was markedly reduced, but in the presence of nicorandil the amplitude was only slightly reduced, consistent with the same increase in ionic conductance and hyperpolarization of the membrane. These results indicate that ATP and nicorandil hyperpolarize the membrane by activating different K-channels, i.e. Ca dependent and Ca insensitive K channels, respectively. As assessed from the effects of local anaesthetics and the membrane properties, the circular muscle may also possess other K channels different from the ATP and nicorandil sensitive K channels.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 250 (1996), S. 241-251 
    ISSN: 1617-4623
    Keywords: mukF ; mukE ; Chromosome partitioning ; Leucine zipper ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have previously reported that the MukB protein is essential for chromosome partitioning inEscherichia coli and thatmukB mutants produce anucleate cells and are temperature-sensitive for colony formation. ThemukB gene maps at 21 min on theE. coli chromosome andsmtA-mukF-mukE-mukB genes might comprise an operon, which is transcribed in a clockwise direction. Here, we report thatmukF andmukE null mutants are both temperature-sensitive for colony formation and produce anucleate cells even at the permissive temperature. These phenotypes are the same as those observed in themukB null mutant. The primary sequence of MukF includes a leucine zipper structure and an acidic domain. Mutational analysis revealed that both are required for MukF function. When the MukF protein was overproduced in the wild-type strain, anucleate cells were produced. In contrast, overproduction of either MukE or MukB did not cause the defect. In null mutants for themukF, mukE, andmukB genes, the synchronous initiation of chromosome replication was not affected. The mini-F plasmid was as stably maintained in these mutants as in the wild-type strain. These results indicate that the MukF, MukE, and MukB proteins are involved in the chromosome partitioning steps, but are not required for mini-F plasmid partitioning.
    Type of Medium: Electronic Resource
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