human apo transferrin  (Millipore)


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    Name:
    Transferrin
    Description:
    Transferrin is a serum glycoprotein that participates in the transport of iron from absorption and storage sites to tissue cells The iron bound transferrin also referred to as ferrotransferrin binds to specific cell surface receptors on growing cells and are internalized by endocytosis Once inside the iron is released into the cells and the iron free transferrin also referred to as apotransferrin is exocytosed outside the cell without being degraded
    Catalog Number:
    10652202001
    Price:
    None
    Applications:
    Transferrin, similar to insulin, is a component of most serum-free media formulations. The main function of transferrin is to transport iron into cells by receptor-mediated endocytosis.Transferrin from human serum has been used as a supplement in:. differentiation medium. keratinocyte medium. haemogenic endothelium culture medium. embryoid-body medium. blast colony forming cell-culture medium
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    Structured Review

    Millipore human apo transferrin
    ESI-MS spectrum of pure <t>apo-transferrin</t> (left) and incubated with RAPTA-T for 1 h at 37 °C at a metallodrug : protein ratio of 5 : 1 (right). Stars indicate the additional peaks caused by the adduct formation.
    Transferrin is a serum glycoprotein that participates in the transport of iron from absorption and storage sites to tissue cells The iron bound transferrin also referred to as ferrotransferrin binds to specific cell surface receptors on growing cells and are internalized by endocytosis Once inside the iron is released into the cells and the iron free transferrin also referred to as apotransferrin is exocytosed outside the cell without being degraded
    https://www.bioz.com/result/human apo transferrin/product/Millipore
    Average 99 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    human apo transferrin - by Bioz Stars, 2020-10
    99/100 stars

    Images

    1) Product Images from "Reactivity of anticancer metallodrugs with serum proteins: new insights from size exclusion chromatography-ICP-MS and ESI-MS †"

    Article Title: Reactivity of anticancer metallodrugs with serum proteins: new insights from size exclusion chromatography-ICP-MS and ESI-MS †

    Journal: Journal of analytical atomic spectrometry

    doi: 10.1039/B922701F

    ESI-MS spectrum of pure apo-transferrin (left) and incubated with RAPTA-T for 1 h at 37 °C at a metallodrug : protein ratio of 5 : 1 (right). Stars indicate the additional peaks caused by the adduct formation.
    Figure Legend Snippet: ESI-MS spectrum of pure apo-transferrin (left) and incubated with RAPTA-T for 1 h at 37 °C at a metallodrug : protein ratio of 5 : 1 (right). Stars indicate the additional peaks caused by the adduct formation.

    Techniques Used: Mass Spectrometry, Incubation

    2) Product Images from "Computational Modeling and Analysis of Iron Release from Macrophages"

    Article Title: Computational Modeling and Analysis of Iron Release from Macrophages

    Journal: PLoS Computational Biology

    doi: 10.1371/journal.pcbi.1003701

    Schematic representation of iron kinetics in solution. Reactions when ferrous ion is added to a solution containing Cp and apo-Tf. Ferrous ion is oxidized by molecular O 2 and ferroxidase Cp. Ferric ion binds to apo-Tf to form mono-ferric ((Fe 3+ )Tf) and di-ferric transferrin ((Fe 3+ ) 2 Tf).
    Figure Legend Snippet: Schematic representation of iron kinetics in solution. Reactions when ferrous ion is added to a solution containing Cp and apo-Tf. Ferrous ion is oxidized by molecular O 2 and ferroxidase Cp. Ferric ion binds to apo-Tf to form mono-ferric ((Fe 3+ )Tf) and di-ferric transferrin ((Fe 3+ ) 2 Tf).

    Techniques Used:

    3) Product Images from "Combining antibiotics with antivirulence compounds can have synergistic effects and reverse selection for antibiotic resistance in Pseudomonas aeruginosa"

    Article Title: Combining antibiotics with antivirulence compounds can have synergistic effects and reverse selection for antibiotic resistance in Pseudomonas aeruginosa

    Journal: PLoS Biology

    doi: 10.1371/journal.pbio.3000805

    Dose-response curves for P . aeruginosa PAO1 under antibiotic-antivirulence combination treatments. Dose-response curves for growth and virulence factor production for PAO1 were assessed for 9×9 drug concentration matrixes involving the four antibiotics combined with either gallium ( A ) or furanone C-30 ( B ). Experiments were carried out in media in which the corresponding virulence factors are required for growth (pyoverdine: CAA+Tf; protease: CAS). Growth and virulence factor production were measured after 48 hours. All values are scaled relative to the untreated control, and data points show the mean across 12 replicates from two independent experiments. We used spline functions to fit the dose-response curves. The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; Tf, human apo-transferrin.
    Figure Legend Snippet: Dose-response curves for P . aeruginosa PAO1 under antibiotic-antivirulence combination treatments. Dose-response curves for growth and virulence factor production for PAO1 were assessed for 9×9 drug concentration matrixes involving the four antibiotics combined with either gallium ( A ) or furanone C-30 ( B ). Experiments were carried out in media in which the corresponding virulence factors are required for growth (pyoverdine: CAA+Tf; protease: CAS). Growth and virulence factor production were measured after 48 hours. All values are scaled relative to the untreated control, and data points show the mean across 12 replicates from two independent experiments. We used spline functions to fit the dose-response curves. The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; Tf, human apo-transferrin.

    Techniques Used: Concentration Assay

    Antivirulence dose response curves for P . aeruginosa PAO1 (growth and virulence factor production). We exposed PAO1 to the antivirulence compounds gallium (inhibiting pyoverdine-mediated iron uptake) and furanone C-30 (blocking QS response, including protease production) both in media in which the targeted virulence factors are expressed and required (iron-limited CAA+Tf medium for gallium and CAS medium for furanone) and in control media, in which the targeted virulence factors are not required (iron-supplemented CAA+Fe medium for gallium and protein digested CAA for furanone). ( A ) Dose-response curves for growth show that both antivirulence compounds reduced bacterial growth, but more so in media in which the targeted virulence factor is expressed. This demonstrates that there is a concentration window where the antivirulence compounds have no toxic effects on bacterial cells and just limit growth due to virulence factor quenching. ( B ) Dose-response curves for virulence factor production show that gallium and furanone C-30 effectively inhibit pyoverdine and protease production, respectively, in a concentration-dependent manner. Dots show means ± standard errors across six replicates. All data are scaled relative to the drug-free treatment. Data stem from two independent experiments using different dilution series. The red dots indicate the highest concentration used for the respective experiments, from which 7 serial dilution steps were tested. Curves were fitted with either log-logistic functions (in CAA+Tf) or with three-parameter Weibull functions (in CAS). The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; QS, quorum sensing; Tf, human apo-transferrin.
    Figure Legend Snippet: Antivirulence dose response curves for P . aeruginosa PAO1 (growth and virulence factor production). We exposed PAO1 to the antivirulence compounds gallium (inhibiting pyoverdine-mediated iron uptake) and furanone C-30 (blocking QS response, including protease production) both in media in which the targeted virulence factors are expressed and required (iron-limited CAA+Tf medium for gallium and CAS medium for furanone) and in control media, in which the targeted virulence factors are not required (iron-supplemented CAA+Fe medium for gallium and protein digested CAA for furanone). ( A ) Dose-response curves for growth show that both antivirulence compounds reduced bacterial growth, but more so in media in which the targeted virulence factor is expressed. This demonstrates that there is a concentration window where the antivirulence compounds have no toxic effects on bacterial cells and just limit growth due to virulence factor quenching. ( B ) Dose-response curves for virulence factor production show that gallium and furanone C-30 effectively inhibit pyoverdine and protease production, respectively, in a concentration-dependent manner. Dots show means ± standard errors across six replicates. All data are scaled relative to the drug-free treatment. Data stem from two independent experiments using different dilution series. The red dots indicate the highest concentration used for the respective experiments, from which 7 serial dilution steps were tested. Curves were fitted with either log-logistic functions (in CAA+Tf) or with three-parameter Weibull functions (in CAS). The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; QS, quorum sensing; Tf, human apo-transferrin.

    Techniques Used: Blocking Assay, Concentration Assay, Serial Dilution

    4) Product Images from "Iron Source Preference and Regulation of Iron Uptake in Cryptococcus neoformans"

    Article Title: Iron Source Preference and Regulation of Iron Uptake in Cryptococcus neoformans

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.0040045

    CFT1 Is Required for Reductive Iron Uptake (A) Iron-starved strains (the wild-type, the cft1 mutant and the CFT1 reconstituted strain) were inoculated into media containing FeCl 3 , apo-transferrin or holo-transferrin, which were added in stepwise 2-fold dilutions. The actual range of concentrations in the cultures was between 200 μM and 0.78 μM of FeCl3, and 20 μM and 0.078 μM of apo- or holo-transferrin. The OD620 reading at 0.1 μM in FeCl3 containing plates and 0.01 μM in Apo- or Holo-transferrin containing plates represent the level of growth in media without an added iron source, starting at the standard inoculum density of 0.08. All cultures were incubated at 30°C and turbidity was measured after 72 h. The averages of three independent experiments are presented with bars representing the standard deviations. (B) The same experiments as shown in (A) were performed for the cft2 mutant and all strains showed similar patterns of growth.
    Figure Legend Snippet: CFT1 Is Required for Reductive Iron Uptake (A) Iron-starved strains (the wild-type, the cft1 mutant and the CFT1 reconstituted strain) were inoculated into media containing FeCl 3 , apo-transferrin or holo-transferrin, which were added in stepwise 2-fold dilutions. The actual range of concentrations in the cultures was between 200 μM and 0.78 μM of FeCl3, and 20 μM and 0.078 μM of apo- or holo-transferrin. The OD620 reading at 0.1 μM in FeCl3 containing plates and 0.01 μM in Apo- or Holo-transferrin containing plates represent the level of growth in media without an added iron source, starting at the standard inoculum density of 0.08. All cultures were incubated at 30°C and turbidity was measured after 72 h. The averages of three independent experiments are presented with bars representing the standard deviations. (B) The same experiments as shown in (A) were performed for the cft2 mutant and all strains showed similar patterns of growth.

    Techniques Used: Mutagenesis, Incubation

    5) Product Images from "In Vitro Antimicrobial Activity of a Siderophore Cephalosporin, S-649266, against Enterobacteriaceae Clinical Isolates, Including Carbapenem-Resistant Strains"

    Article Title: In Vitro Antimicrobial Activity of a Siderophore Cephalosporin, S-649266, against Enterobacteriaceae Clinical Isolates, Including Carbapenem-Resistant Strains

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.01695-15

    Cumulative percentage of MICs against meropenem-resistant carbapenemase-producing Enterobacteriaceae . The test strains were 110 E. coli , K. pneumoniae , S. marcescens , C. freundii , and E. cloacae isolates that consisted of 40 KPC-type-, 47 NDM-1-, 7 VIM-type-, 7 IMP-type-, 6 SME-type-, 1 NMC-A-, and 2 OXA-48-producing strains. Cation-adjusted Mueller-Hinton broth was used as a medium, but 20 μM human apo-transferrin was supplemented for the MIC determination of S-649266 to obtain a free iron-deficient condition. The broken lines represent 50% and 90% lines.
    Figure Legend Snippet: Cumulative percentage of MICs against meropenem-resistant carbapenemase-producing Enterobacteriaceae . The test strains were 110 E. coli , K. pneumoniae , S. marcescens , C. freundii , and E. cloacae isolates that consisted of 40 KPC-type-, 47 NDM-1-, 7 VIM-type-, 7 IMP-type-, 6 SME-type-, 1 NMC-A-, and 2 OXA-48-producing strains. Cation-adjusted Mueller-Hinton broth was used as a medium, but 20 μM human apo-transferrin was supplemented for the MIC determination of S-649266 to obtain a free iron-deficient condition. The broken lines represent 50% and 90% lines.

    Techniques Used:

    Related Articles

    other:

    Article Title: Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates
    Article Snippet: Transferrin, glycine, ammonium persulfate, tetramethylammonium chloride, tetrabutylammonium hydroxide, zirconyl chloride octahydrate, zirconium(IV) chloride, sodium phosphate dibasic and deuterium oxide were bought from Sigma-Aldrich (St. Louis, MO, USA).

    Polyacrylamide Gel Electrophoresis:

    Article Title: Targeted Delivery of Amoxicillin to C. trachomatis by the Transferrin Iron Acquisition Pathway
    Article Snippet: .. Purification of transferrin and receptor At least 98%-pure human-serum apotransferrin (Sigma) was further purified according to published procedures [ , ]; its purity was checked both spectrophotometrically and by urea polyacrylamide gel electrophoresis [ ]. .. Holotransferrin (Tf), was prepared and purified as described elsewhere [ ].

    Purification:

    Article Title: Targeted Delivery of Amoxicillin to C. trachomatis by the Transferrin Iron Acquisition Pathway
    Article Snippet: .. Purification of transferrin and receptor At least 98%-pure human-serum apotransferrin (Sigma) was further purified according to published procedures [ , ]; its purity was checked both spectrophotometrically and by urea polyacrylamide gel electrophoresis [ ]. .. Holotransferrin (Tf), was prepared and purified as described elsewhere [ ].

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    Millipore apo transferrin
    Dose-response curves for P . aeruginosa PAO1 under antibiotic-antivirulence combination treatments. Dose-response curves for growth and virulence factor production for PAO1 were assessed for 9×9 drug concentration matrixes involving the four antibiotics combined with either gallium ( A ) or furanone C-30 ( B ). Experiments were carried out in media in which the corresponding virulence factors are required for growth (pyoverdine: CAA+Tf; protease: CAS). Growth and virulence factor production were measured after 48 hours. All values are scaled relative to the untreated control, and data points show the mean across 12 replicates from two independent experiments. We used spline functions to fit the dose-response curves. The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; Tf, human <t>apo-transferrin.</t>
    Apo Transferrin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 107 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/apo transferrin/product/Millipore
    Average 99 stars, based on 107 article reviews
    Price from $9.99 to $1999.99
    apo transferrin - by Bioz Stars, 2020-10
    99/100 stars
      Buy from Supplier

    99
    Millipore human apo transferrin
    Schematic representation of iron kinetics in solution. Reactions when ferrous ion is added to a solution containing Cp and <t>apo-Tf.</t> Ferrous ion is oxidized by molecular O 2 and ferroxidase Cp. Ferric ion binds to apo-Tf to form mono-ferric ((Fe 3+ )Tf) and di-ferric <t>transferrin</t> ((Fe 3+ ) 2 Tf).
    Human Apo Transferrin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human apo transferrin/product/Millipore
    Average 99 stars, based on 24 article reviews
    Price from $9.99 to $1999.99
    human apo transferrin - by Bioz Stars, 2020-10
    99/100 stars
      Buy from Supplier

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    Dose-response curves for P . aeruginosa PAO1 under antibiotic-antivirulence combination treatments. Dose-response curves for growth and virulence factor production for PAO1 were assessed for 9×9 drug concentration matrixes involving the four antibiotics combined with either gallium ( A ) or furanone C-30 ( B ). Experiments were carried out in media in which the corresponding virulence factors are required for growth (pyoverdine: CAA+Tf; protease: CAS). Growth and virulence factor production were measured after 48 hours. All values are scaled relative to the untreated control, and data points show the mean across 12 replicates from two independent experiments. We used spline functions to fit the dose-response curves. The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; Tf, human apo-transferrin.

    Journal: PLoS Biology

    Article Title: Combining antibiotics with antivirulence compounds can have synergistic effects and reverse selection for antibiotic resistance in Pseudomonas aeruginosa

    doi: 10.1371/journal.pbio.3000805

    Figure Lengend Snippet: Dose-response curves for P . aeruginosa PAO1 under antibiotic-antivirulence combination treatments. Dose-response curves for growth and virulence factor production for PAO1 were assessed for 9×9 drug concentration matrixes involving the four antibiotics combined with either gallium ( A ) or furanone C-30 ( B ). Experiments were carried out in media in which the corresponding virulence factors are required for growth (pyoverdine: CAA+Tf; protease: CAS). Growth and virulence factor production were measured after 48 hours. All values are scaled relative to the untreated control, and data points show the mean across 12 replicates from two independent experiments. We used spline functions to fit the dose-response curves. The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; Tf, human apo-transferrin.

    Article Snippet: As an iron-rich control medium, we used CAA supplemented with 25 mM HEPES and 20 μM FeCl3 , but without apo-transferrin and 20 mM NaHCO3 to create conditions that do not require pyoverdine for growth [ ].

    Techniques: Concentration Assay

    Antivirulence dose response curves for P . aeruginosa PAO1 (growth and virulence factor production). We exposed PAO1 to the antivirulence compounds gallium (inhibiting pyoverdine-mediated iron uptake) and furanone C-30 (blocking QS response, including protease production) both in media in which the targeted virulence factors are expressed and required (iron-limited CAA+Tf medium for gallium and CAS medium for furanone) and in control media, in which the targeted virulence factors are not required (iron-supplemented CAA+Fe medium for gallium and protein digested CAA for furanone). ( A ) Dose-response curves for growth show that both antivirulence compounds reduced bacterial growth, but more so in media in which the targeted virulence factor is expressed. This demonstrates that there is a concentration window where the antivirulence compounds have no toxic effects on bacterial cells and just limit growth due to virulence factor quenching. ( B ) Dose-response curves for virulence factor production show that gallium and furanone C-30 effectively inhibit pyoverdine and protease production, respectively, in a concentration-dependent manner. Dots show means ± standard errors across six replicates. All data are scaled relative to the drug-free treatment. Data stem from two independent experiments using different dilution series. The red dots indicate the highest concentration used for the respective experiments, from which 7 serial dilution steps were tested. Curves were fitted with either log-logistic functions (in CAA+Tf) or with three-parameter Weibull functions (in CAS). The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; QS, quorum sensing; Tf, human apo-transferrin.

    Journal: PLoS Biology

    Article Title: Combining antibiotics with antivirulence compounds can have synergistic effects and reverse selection for antibiotic resistance in Pseudomonas aeruginosa

    doi: 10.1371/journal.pbio.3000805

    Figure Lengend Snippet: Antivirulence dose response curves for P . aeruginosa PAO1 (growth and virulence factor production). We exposed PAO1 to the antivirulence compounds gallium (inhibiting pyoverdine-mediated iron uptake) and furanone C-30 (blocking QS response, including protease production) both in media in which the targeted virulence factors are expressed and required (iron-limited CAA+Tf medium for gallium and CAS medium for furanone) and in control media, in which the targeted virulence factors are not required (iron-supplemented CAA+Fe medium for gallium and protein digested CAA for furanone). ( A ) Dose-response curves for growth show that both antivirulence compounds reduced bacterial growth, but more so in media in which the targeted virulence factor is expressed. This demonstrates that there is a concentration window where the antivirulence compounds have no toxic effects on bacterial cells and just limit growth due to virulence factor quenching. ( B ) Dose-response curves for virulence factor production show that gallium and furanone C-30 effectively inhibit pyoverdine and protease production, respectively, in a concentration-dependent manner. Dots show means ± standard errors across six replicates. All data are scaled relative to the drug-free treatment. Data stem from two independent experiments using different dilution series. The red dots indicate the highest concentration used for the respective experiments, from which 7 serial dilution steps were tested. Curves were fitted with either log-logistic functions (in CAA+Tf) or with three-parameter Weibull functions (in CAS). The underlying data for this figure can be found at https://doi.org/10.6084/m9.figshare.12515364 . CAA, casamino acid medium; CAS, casein medium; QS, quorum sensing; Tf, human apo-transferrin.

    Article Snippet: As an iron-rich control medium, we used CAA supplemented with 25 mM HEPES and 20 μM FeCl3 , but without apo-transferrin and 20 mM NaHCO3 to create conditions that do not require pyoverdine for growth [ ].

    Techniques: Blocking Assay, Concentration Assay, Serial Dilution

    Schematic representation of iron kinetics in solution. Reactions when ferrous ion is added to a solution containing Cp and apo-Tf. Ferrous ion is oxidized by molecular O 2 and ferroxidase Cp. Ferric ion binds to apo-Tf to form mono-ferric ((Fe 3+ )Tf) and di-ferric transferrin ((Fe 3+ ) 2 Tf).

    Journal: PLoS Computational Biology

    Article Title: Computational Modeling and Analysis of Iron Release from Macrophages

    doi: 10.1371/journal.pcbi.1003701

    Figure Lengend Snippet: Schematic representation of iron kinetics in solution. Reactions when ferrous ion is added to a solution containing Cp and apo-Tf. Ferrous ion is oxidized by molecular O 2 and ferroxidase Cp. Ferric ion binds to apo-Tf to form mono-ferric ((Fe 3+ )Tf) and di-ferric transferrin ((Fe 3+ ) 2 Tf).

    Article Snippet: Human apo-transferrin was obtained from Calbiochem (Billerica, MA).

    Techniques:

    Identification of human transferrin as the bacteriostatic component. A , functional screening of serum fractions prepared by gel filtration. Fractions were incubated with B. anthracis Sterne 7702 for 12 h and subsequently subcultured in THB to assess growth after 7 h by A 600 . Inlay, below : immunoblot analysis of fraction 13–20 using an anti-human transferrin antibody. Representative figures of two independent experiments. B , growth of B. anthracis Sterne 34F2 after 5 h of incubation with 0, 1, 10, or 100 μg/ml human apo-transferrin. C , growth of B. anthracis Ames after 5 h of incubation with 100 μg/ml human apo-transferrin (apo-hTF). *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Human Transferrin Confers Serum Resistance against Bacillus anthracis *

    doi: 10.1074/jbc.M110.154930

    Figure Lengend Snippet: Identification of human transferrin as the bacteriostatic component. A , functional screening of serum fractions prepared by gel filtration. Fractions were incubated with B. anthracis Sterne 7702 for 12 h and subsequently subcultured in THB to assess growth after 7 h by A 600 . Inlay, below : immunoblot analysis of fraction 13–20 using an anti-human transferrin antibody. Representative figures of two independent experiments. B , growth of B. anthracis Sterne 34F2 after 5 h of incubation with 0, 1, 10, or 100 μg/ml human apo-transferrin. C , growth of B. anthracis Ames after 5 h of incubation with 100 μg/ml human apo-transferrin (apo-hTF). *, p

    Article Snippet: Human apo-transferrin (apo-hTF) and holo-transferrin (holo-hTF) were obtained from Calbiochem (San Diego, CA).

    Techniques: Functional Assay, Filtration, Incubation

    Transferrin blocks growth of B. anthracis by iron deprivation. A , growth of B. anthracis Sterne 34F2 after 5 h of incubation with human apo-transferrin (apo-hTF, iron-free) or holo-transferrin (holo-hTF, iron-saturated). B , growth of B. anthracis Sterne 34F2 after 5 h of incubation in the presence of recombinant apo-transferrin ( apo-rhTF ), recombinant holo-transferrin ( holo-rhTF ), or apo-rhTF mutated in its iron-binding sites ( apo-rhTF Δ Fe ). C , growth of B. anthracis Sterne 34F2 after 5 h of incubation in the presence of human serum (0 or 10%) in the presence of iron(III) citrate. D , relative growth of different Gram-positive pathogens grown for 5 h in the presence of human apo-transferrin (apo-hTF). Growth in buffer alone was set at 100%. Data represent mean ± S.E. of three independent experiments. Growth indices indicate ratio of bacterial cfu surviving after incubation versus the initial inoculum. **, p

    Journal: The Journal of Biological Chemistry

    Article Title: Human Transferrin Confers Serum Resistance against Bacillus anthracis *

    doi: 10.1074/jbc.M110.154930

    Figure Lengend Snippet: Transferrin blocks growth of B. anthracis by iron deprivation. A , growth of B. anthracis Sterne 34F2 after 5 h of incubation with human apo-transferrin (apo-hTF, iron-free) or holo-transferrin (holo-hTF, iron-saturated). B , growth of B. anthracis Sterne 34F2 after 5 h of incubation in the presence of recombinant apo-transferrin ( apo-rhTF ), recombinant holo-transferrin ( holo-rhTF ), or apo-rhTF mutated in its iron-binding sites ( apo-rhTF Δ Fe ). C , growth of B. anthracis Sterne 34F2 after 5 h of incubation in the presence of human serum (0 or 10%) in the presence of iron(III) citrate. D , relative growth of different Gram-positive pathogens grown for 5 h in the presence of human apo-transferrin (apo-hTF). Growth in buffer alone was set at 100%. Data represent mean ± S.E. of three independent experiments. Growth indices indicate ratio of bacterial cfu surviving after incubation versus the initial inoculum. **, p

    Article Snippet: Human apo-transferrin (apo-hTF) and holo-transferrin (holo-hTF) were obtained from Calbiochem (San Diego, CA).

    Techniques: Incubation, Recombinant, Binding Assay