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  • 1
    Electronic Resource
    Electronic Resource
    Chromosome-mediated resistance of Yersinia enterocolitica serotype O9 to intracellular killing by mouse peritoneal macrophages (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 9 (1994), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract The survival of Yersinia enterocolitica serotype O9 within mouse peritoneal macrophages was investigated. To evaluate the role of the virulence plasmid in the resistance to intracellular killing, an isogenic pair of virulent (plasmid-bearing) and avirulent (plasmid-less) O9 strains was used. The virulent strain was able to express plasmid-encoded outer membrane proteins and to colonize the Peyer's patches of orally infected mice. When mice were infected intraperitoneally, both strains were recovered at similar rates and over the same time from the peritoneal cavity. When in vitro assays were performed, both strains showed similar resistance to intracellular killing by monolayers of resident and inflammatory peritoneal macrophages. Previous opsonization of bacteria did not modify their survival within macrophage monolayers. We concluded that serotype O9 strains display a chromosome-mediated resistance to intracellular killing by mouse peritoneal macrophages. Moreover, macrophage resistance does not seem to be of importance for virulence of serotype O9 strains in mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1994.tb00367.x
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  • 2
    Electronic Resource
    Electronic Resource
    Uptake and decarboxylation of indole-3-acetic acid during auxin-induced growth in lupin hypocotyl segments (1994)
    Springer
    Planta 193 (1994), S. 224-231 
    Details
    ISSN: 1432-2048
    Keywords: Acid-growth theory ; ATPase ; auxin (uptake, decarboxylation) ; Growth (auxin induced) ; Lupinus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The elongation growth of etiolated hypocotyl segments of lupin (Lupinus albus L.) was stimulated by acid pH (4.6 versus 6.5) and by IAA for periods of up to 4 h. After this time, the segments were unable to grow further. In the presence of an optimal IAA concentration (10 μM), acid pH increased the growth rate but had no effect on final growth. With suboptimal IAA (0.1 μM), however, acid pH increased growth in a more than additive way, suggesting a synergistic action between the two factors. This synergism may be explained by the increased IAA uptake and decarboxylation seen at an acid pH. These results reinforce the view that the effects of low pH and IAA on growth are not independent. Vanadate inhibited growth and also IAA uptake and decarboxylation. This inhibitor, therefore, probably inhibits growth not only by decreasing ATPase-mediated acidification but also by decreasing H+-dependent IAA uptake from the apoplasm. This dependence of IAA uptake on ATPase may be mediated by apoplasmic acidification. The amount of IAA decarboxylated increased when the assay conditions favored the growth of segments, indicating that IAA could be destroyed by decarboxylation during the auxin-induced growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00192534
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  • 3
    Electronic Resource
    Electronic Resource
    A genetic approach to the identification of functional amino acids in protein p6 of Bacillus subtilis phage ø29 (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 529-536 
    Details
    ISSN: 1617-4623
    Keywords: Trans-complementation ; In vivo DNA replication ; Phage ø29 ; Site-directed mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein p6 of the Bacillus subtilis phage ø29 is essential for in vivo viral DNA replication. This protein activates the initiation of ø29 DNA replication in vitro by forming a multimeric nucleoprotein complex at the replication origins. The N-terminal region of protein p6 is involved in DNA binding, as shown by in vitro studies with p6 proteins altered by deletions or missense mutations. We report on the development of an in vivo functional assay for protein p6. This assay is based on the ability of protein p6-producing B. subtilis non-suppressor (su −) cells to support growth of a ø29 sus6 mutant phage. We have used this trans-complementation assay to investigate the effect on in vivo viral DNA synthesis of missense mutations introduced into the protein p6 N-terminal region. The alteration of lysine to alanine at position 2 resulted in a partially functional protein, whereas the replacement of arginine by alanine at position 6 gave rise to an inactive protein. These results indicate that arginine at position 6 is critical for the in vivo activity of protein p6. Our complementation system provides a useful genetic approach for the identification of functionally important amino acids in protein p6.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00282215
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  • 4
    Electronic Resource
    Electronic Resource
    Triphenyltin as inductor of mitochondrial membrane permeability transition (1994)
    Springer
    Journal of bioenergetics and biomembranes 26 (1994), S. 457-462 
    Details
    ISSN: 1573-6881
    Keywords: Triphenyltin ; mitochondrial Ca2+ ; trialkytin compound
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of triphenyltin on mitochondrial Ca2+ content was studied. It was found that this trialkyltin compound induces an increase in membrane permeability that leads to Ca2+ release, drop of the transmembrane potential, and efflux of matrix proteins. Interestingly, cyclosporin A was unable to inhibit triphenyltin-induced Ca2+ release. Based on these results it is proposed that the hyperpermeable state is produced by modification of 2.25 nmol of membrane thiol groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762786
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  • 5
    Electronic Resource
    Electronic Resource
    Identification of a 20-kDa protein with calcium uptake transport activity. Reconstitution in a membrane model (1994)
    Springer
    Journal of bioenergetics and biomembranes 26 (1994), S. 555-562 
    Details
    ISSN: 1573-6881
    Keywords: Calcium uptake ; uniporter ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract This paper presents results of experiments designed to further purify the membrane system involved in mitochondrial calcium transport. A partially purified extract, which transported calcium with a specific activity of 1194 nmol45Ca2+/mg protein/5 min, was used to obtain mouse hyperimmune serum. This serum inhibited calcium uptake both in mitoplasts and in vesicles reconstituted with mitochondrial proteins containing cytochrome oxidase. Western blot analysis of the semipurified fraction showed that the serum recognized specifically two antigens of 75 and 20 kDa. Both antibodies were purified by elution from the nitrocellulose sheets and their inhibition capacity was analyzed. The antibody that recognized the 20-kDa protein produced a higher degree of inhibition than the other one.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762740
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