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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 23 (1994), S. 155-165 
    ISSN: 1432-1017
    Keywords: Alamethicin ; Ion channel blockade ; Planar lipid bilayers ; Polycations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The effects of the peptide polycations salmon protamine (M r = 4332,z = + 21) and poly-l-lysine (M r ≅ 100,00,z ≅ + 775) on ion channels formed by synthetic alamethicin Alm-F30 (one negative charge), natural Alm-F50 (neutral) and phosphorylated Alm-F50 (two negative charges) reconstituted in planar lipid bilayers have been studied at the single channel level. It was observed that both polycations in micromolar concentrations transiently block ion permeation through the channels formed by each alamethicin analogue, although in case of the neutral Alm-F50 to a significantly lesser extent. Poly-l-lysine showed to be more effective than protamine in blocking these channels. If either polycation is present in the cis-compartment, blockade occurs only at cis positive membrane voltages. At constant polycation concentration, dwell times in the blocked state increase when salt concentration is lowered, and decrease at acidic pH with an apparent pK of 4.8. Mean lifetime of blockade events shortens when membrane voltage is increased, which suggests that both polycations may permeate through the oligomeric alamethicin channels if conductance levels are 〉 2. We suggest that blockade is caused by electrostatic binding of a single polycation molecule to the C-terminal channel mouth; in case of Alm-F30, Glu18 has to be considered as the putative binding site. Our results provide further evidence for the barrel-stave model and a parallel orientation of dipole monomers in the channel aggregate, the C-termini facing the membrane side with the more positive membrane potential.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 115 (1994), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A highly hydrophilic compound with siderophore activity has been isolated from the supernatant of Staphylococcus hyicus DSM 20459 grown under iron-restricted conditions. The metabolite, named staphyloferrin B, is strictly iron-regulated and produced by a large variety of staphylococci strains. In vivo iron transport measurements and the growth-promoting activity in a bioassay establish staphyloferrin B as the second siderophore for staphylococci besides the previously described staphyloferrin A. The structure elucidation revealed 2,3-diaminopropionic acid, citrate, ethylenediamine and 2-ketoglutaric acid as structural components of the compound. Thus, staphyloferrin B is a structurally new siderophore of the complexone type.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 8 (1994), S. 0 
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract The production of TNF-α, IL-1 and IL-6 was measured in mice after i.p. injections of the synthetic bacterial lipopeptide Pam3Cys-Ala-Gly, a potent macrophage and B cell activator in vitro. Only minor amounts of IL-6 and no TNF-α were detectable in the serum of mice injected with 10 or 100 μg of Pam3Cys-Ala-Gly. Lipopeptide concentrations up to 1000 μg failed to induce IL-1, and TNF-α production and serum IL-6 levels were only slightly elevated. In contrast to Pam3Cys-Ala-Gly, i.p. injections of LPS were accompanied by high levels of the inflammatory cytokines TNF-α, IL-1 and IL-6 suggesting fundamental differences of the mode of action of these two substances when applied in vivo.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The use of a phosphate organic form taken up by Kluyveromyces lactis removes repression of the PHO5 promoter and releases heterologous interleukin 1β synthesis while providing sufficient phosphate for growth. The oxidative metabolism of high-cell-density fed-batch and chemostat cultures was thus maintained under derepressed protein synthesis conditions. Interleukin 1β production was then growth-associated, an unusual mode of protein synthesis regulation under the control of the PHO5 promoter.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The use of a phosphate organic form taken up by Kluyveromyces lactis removes repression of the PHO5 promoter and releases heterologous interleukin 1\ synthesis while providing sufficient phosphate for growth. The oxidative metabolism of high-cell-density fed-batch and chemostat cultures was thus maintained under derepressed protein synthesis conditions. Interleukin 1\ production was then growth-associated, an unusual mode of protein synthesis regulation under the control of the PHO5 promoter.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0749-503X
    Keywords: Yeast ; Kluyveromyces lactis ; recombinant ; phosphoglycerate kinase ; glycolysis ; heterologous protein ; rHSA ; chemostat culture ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Production of recombinant human serum albumin (rHSA) controlled by the constitutive promoter phosphoglycerate kinase was studied in Kluyveromyces lactis. It was governed by both cell concentration and glycolytic flow. The triggering of the fermentation metabolism by unfavourable culture conditions (pH, pO2, D) caused a decrease in the synthesis of the heterologous protein. The highest productivity (75 mg 1-1 per h) and rHSA concentration (62 mg 1-1) were obtained in chemostat culture with a dilution rate of 0·12 h-1 and with 38 g 1-1 dry weight.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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