colorimetric nitrocefin disk assay  (Thermo Fisher)


Bioz Verified Symbol Thermo Fisher is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 85

    Structured Review

    Thermo Fisher colorimetric nitrocefin disk assay
    Colorimetric Nitrocefin Disk Assay, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/colorimetric nitrocefin disk assay/product/Thermo Fisher
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    colorimetric nitrocefin disk assay - by Bioz Stars, 2020-09
    85/100 stars

    Images

    Related Articles

    Beta Lactamase Assay:

    Article Title: Genetic Diversity among Enterococcus faecalis
    Article Snippet: .. β-lactamase assay Direct assessment of β-lactamase activity was performed using the colorimetric Nitrocefin disk assay (Remel Co., U.K.), per manufacturer's instructions. .. Cytolysin assay Blood agar plates were used for the qualitative detection of hemolytic activity.

    Activity Assay:

    Article Title: Genetic Diversity among Enterococcus faecalis
    Article Snippet: .. β-lactamase assay Direct assessment of β-lactamase activity was performed using the colorimetric Nitrocefin disk assay (Remel Co., U.K.), per manufacturer's instructions. .. Cytolysin assay Blood agar plates were used for the qualitative detection of hemolytic activity.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90
    Thermo Fisher nitrocefin
    Kinetics of changes in E. coli ML-35p outer and cytoplasmic membrane permeability measured with the use of chromogenic markers – the products of <t>nitrocefin</t> (OD 540 ) and ONPG (OD 405 ) hydrolysis, respectively. Outer membrane permeability resulting from incubation of bacteria with mini-ChBac7.5Nα at various concentrations (from 0.125 to 32 μM, highlighted with colors) in the absence (A) or in the presence (B) of 0.9% NaCl. Melittin and ChMAP-28 at concentration of 1 μM were used as positive control samples. (C) Analysis of outer membrane permeability resulting from incubation with ChMAP-28 or melittin in the presence of 0.9% NaCl. (D) Comparative analysis of cytoplasmic membrane permeability resulting from incubation with the individual ChMAP-28 or with its combinations with mini-ChBac7.5Nα. Melittin at concentration of 8 μM was used as a positive control. Three independent experiments were performed, and the curve pattern was similar for the three series.
    Nitrocefin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nitrocefin/product/Thermo Fisher
    Average 90 stars, based on 25 article reviews
    Price from $9.99 to $1999.99
    nitrocefin - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    94
    carbosynth nitrocefin
    Biochemical analysis of relebactam inhibition of M. abscessus β -lactamase, Bla Mab . Our novel Thin Layer Chromatography (TLC) assay (2a) exhibiting the activity of Bla Mab in the turnover of penicillin V (high R f value) to penicilloic acid (lower R f value). In the absence, or termination of activity of Bla Mab (by boiling (100 °C) for 1 h) or addition of known inhibitor avibactam ( Lefebvre et al., 2017 ) (200 μg/mL) no lower R f value spot corresponding to penicilloic acid is seen on the TLC plate. The addition of relebactam to the reaction between Bla Mab and penicillin V also results in the absence of the lower Rf value spot, suggesting inhibition of Bla Mab (2a). This observed inhibition is validated by a spectrophotometric analysis, where the turnover of <t>nitrocefin</t> (100 μM) by Bla Mab (0.25 nM) was monitored at 486 nm with a varying concentration of relebactam (0, 0.1, 1, 10 and 100 μM). The increase in concentration of relebactam resulted in partial inhibition of nitrocefin turnover at 1 μM and total abrogation at 10 μM (2b). The initial velocity (v i ) of the reaction between Bla Mab and nitrocefin was monitored for a range of substrate concentrations (1-500 μM) and relebactam concentrations (0, 0.5, 0.75, 1 and 2.5 μM). This data was plotted v i vs [S] in order to determine K m values (2c/f). The values for K obs were obtained as previously described ( Dubée et al., 2014 ) and plotted against relebactam concentrations ([I]) to deduce a carbamylation rate ( K 2 / K i ) for Bla Mab (2d). The kinetics of Bla Mab decarbamylation were assessed to show the recovery of nitrocefin hydrolysis by Bla Mab after inhibition by relebactam in order to derive a K off value (2e). Kinetic parameters were derived as described previously (2f) ( Dubée et al., 2014 ).
    Nitrocefin, supplied by carbosynth, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nitrocefin/product/carbosynth
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    nitrocefin - by Bioz Stars, 2020-09
    94/100 stars
      Buy from Supplier

    Image Search Results


    Kinetics of changes in E. coli ML-35p outer and cytoplasmic membrane permeability measured with the use of chromogenic markers – the products of nitrocefin (OD 540 ) and ONPG (OD 405 ) hydrolysis, respectively. Outer membrane permeability resulting from incubation of bacteria with mini-ChBac7.5Nα at various concentrations (from 0.125 to 32 μM, highlighted with colors) in the absence (A) or in the presence (B) of 0.9% NaCl. Melittin and ChMAP-28 at concentration of 1 μM were used as positive control samples. (C) Analysis of outer membrane permeability resulting from incubation with ChMAP-28 or melittin in the presence of 0.9% NaCl. (D) Comparative analysis of cytoplasmic membrane permeability resulting from incubation with the individual ChMAP-28 or with its combinations with mini-ChBac7.5Nα. Melittin at concentration of 8 μM was used as a positive control. Three independent experiments were performed, and the curve pattern was similar for the three series.

    Journal: Frontiers in Microbiology

    Article Title: Combined Antibacterial Effects of Goat Cathelicidins With Different Mechanisms of Action

    doi: 10.3389/fmicb.2018.02983

    Figure Lengend Snippet: Kinetics of changes in E. coli ML-35p outer and cytoplasmic membrane permeability measured with the use of chromogenic markers – the products of nitrocefin (OD 540 ) and ONPG (OD 405 ) hydrolysis, respectively. Outer membrane permeability resulting from incubation of bacteria with mini-ChBac7.5Nα at various concentrations (from 0.125 to 32 μM, highlighted with colors) in the absence (A) or in the presence (B) of 0.9% NaCl. Melittin and ChMAP-28 at concentration of 1 μM were used as positive control samples. (C) Analysis of outer membrane permeability resulting from incubation with ChMAP-28 or melittin in the presence of 0.9% NaCl. (D) Comparative analysis of cytoplasmic membrane permeability resulting from incubation with the individual ChMAP-28 or with its combinations with mini-ChBac7.5Nα. Melittin at concentration of 8 μM was used as a positive control. Three independent experiments were performed, and the curve pattern was similar for the three series.

    Article Snippet: Peptide samples were placed in the wells of a 96-well plate with non-binding surface (NBS, Corning #3641), and the optical density (OD) of the solution rising due to the appearance of the hydrolyzed nitrocefin or ONPG was measured at 540 and 405 nm, respectively, using the Multiskan EX microplate reader (Thermo Fisher Scientific).

    Techniques: Permeability, Incubation, Concentration Assay, Positive Control

    Nitrocefin degradation assay for E . coli ATCC 35218, 35218R and 35218Δ bla . Nitrocefin degradation by E . coli 35218R (red squares), E . coli ATCC 35218 (black circles) and E . coli 35218Δ bla (green triangles). The absorbance at 480 nm vs. time were modelled by linear regression and compared by curve fitting analysis (CFA). Strain 35218R (red squares and line) hydrolyzed nitrocefin more efficiently than the parental ATCC 35218 (black circles and line), while no hydrolysis occurred with the plasmid-cured isogenic strain 35218Δ bla (green diamonds and line), confirming β-lactamase hyperproduction by E . coli 35218R and negligible β-lactamase activity of E . coli 35218Δ bla . The P value from the slope comparison indicates that each group is described by an independent line.

    Journal: PLoS ONE

    Article Title: Impact on Bacterial Resistance of Therapeutically Nonequivalent Generics: The Case of Piperacillin-Tazobactam

    doi: 10.1371/journal.pone.0155806

    Figure Lengend Snippet: Nitrocefin degradation assay for E . coli ATCC 35218, 35218R and 35218Δ bla . Nitrocefin degradation by E . coli 35218R (red squares), E . coli ATCC 35218 (black circles) and E . coli 35218Δ bla (green triangles). The absorbance at 480 nm vs. time were modelled by linear regression and compared by curve fitting analysis (CFA). Strain 35218R (red squares and line) hydrolyzed nitrocefin more efficiently than the parental ATCC 35218 (black circles and line), while no hydrolysis occurred with the plasmid-cured isogenic strain 35218Δ bla (green diamonds and line), confirming β-lactamase hyperproduction by E . coli 35218R and negligible β-lactamase activity of E . coli 35218Δ bla . The P value from the slope comparison indicates that each group is described by an independent line.

    Article Snippet: The amount of nitrocefin degraded per minute was determined by Beer’s equation with the change in absorbance at OD486nm (Genesys 20 spectrophotometer, Thermo Scientific, USA) and a molar extinction coefficient of 20,500 M-1 .cm-1 , and the result was expressed as the nmol of nitrocefin degraded per minute per mg of protein [ ].

    Techniques: Degradation Assay, Plasmid Preparation, Activity Assay

    Changes in outer and inner membrane permeabilization caused by olanexidine and chlorhexidine in E. coli ML-35p cells incubated in 5 mM HEPES buffer containing 20 μg/ml nitrocefin and 5 μM carbonyl cyanide 3-chlorophenylhydrazone with olanexidine

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Bactericidal Effects and Mechanism of Action of Olanexidine Gluconate, a New Antiseptic

    doi: 10.1128/AAC.05048-14

    Figure Lengend Snippet: Changes in outer and inner membrane permeabilization caused by olanexidine and chlorhexidine in E. coli ML-35p cells incubated in 5 mM HEPES buffer containing 20 μg/ml nitrocefin and 5 μM carbonyl cyanide 3-chlorophenylhydrazone with olanexidine

    Article Snippet: Bodipy TR cadaverine [5-(((4-(4,4-difluoro-5-(2-thienyl)-4-bora-3a,4a-diaza- s -indacene-3-yl)phenoxy)acetyl)amino)–pentylamine, hydrochloride] (BC), lipid A from Escherichia coli strain K-12, and nitrocefin were purchased from Thermo Fisher Scientific, Inc. (Waltham, MA), List Biological Laboratories, Inc. (Campbell, CA), and Merck KGaA (Darmstadt, Germany), respectively.

    Techniques: Incubation

    Biochemical analysis of relebactam inhibition of M. abscessus β -lactamase, Bla Mab . Our novel Thin Layer Chromatography (TLC) assay (2a) exhibiting the activity of Bla Mab in the turnover of penicillin V (high R f value) to penicilloic acid (lower R f value). In the absence, or termination of activity of Bla Mab (by boiling (100 °C) for 1 h) or addition of known inhibitor avibactam ( Lefebvre et al., 2017 ) (200 μg/mL) no lower R f value spot corresponding to penicilloic acid is seen on the TLC plate. The addition of relebactam to the reaction between Bla Mab and penicillin V also results in the absence of the lower Rf value spot, suggesting inhibition of Bla Mab (2a). This observed inhibition is validated by a spectrophotometric analysis, where the turnover of nitrocefin (100 μM) by Bla Mab (0.25 nM) was monitored at 486 nm with a varying concentration of relebactam (0, 0.1, 1, 10 and 100 μM). The increase in concentration of relebactam resulted in partial inhibition of nitrocefin turnover at 1 μM and total abrogation at 10 μM (2b). The initial velocity (v i ) of the reaction between Bla Mab and nitrocefin was monitored for a range of substrate concentrations (1-500 μM) and relebactam concentrations (0, 0.5, 0.75, 1 and 2.5 μM). This data was plotted v i vs [S] in order to determine K m values (2c/f). The values for K obs were obtained as previously described ( Dubée et al., 2014 ) and plotted against relebactam concentrations ([I]) to deduce a carbamylation rate ( K 2 / K i ) for Bla Mab (2d). The kinetics of Bla Mab decarbamylation were assessed to show the recovery of nitrocefin hydrolysis by Bla Mab after inhibition by relebactam in order to derive a K off value (2e). Kinetic parameters were derived as described previously (2f) ( Dubée et al., 2014 ).

    Journal: bioRxiv

    Article Title: Combining amoxicillin and relebactam provides a new therapeutic option for Mycobacterium abscessus infection

    doi: 10.1101/563189

    Figure Lengend Snippet: Biochemical analysis of relebactam inhibition of M. abscessus β -lactamase, Bla Mab . Our novel Thin Layer Chromatography (TLC) assay (2a) exhibiting the activity of Bla Mab in the turnover of penicillin V (high R f value) to penicilloic acid (lower R f value). In the absence, or termination of activity of Bla Mab (by boiling (100 °C) for 1 h) or addition of known inhibitor avibactam ( Lefebvre et al., 2017 ) (200 μg/mL) no lower R f value spot corresponding to penicilloic acid is seen on the TLC plate. The addition of relebactam to the reaction between Bla Mab and penicillin V also results in the absence of the lower Rf value spot, suggesting inhibition of Bla Mab (2a). This observed inhibition is validated by a spectrophotometric analysis, where the turnover of nitrocefin (100 μM) by Bla Mab (0.25 nM) was monitored at 486 nm with a varying concentration of relebactam (0, 0.1, 1, 10 and 100 μM). The increase in concentration of relebactam resulted in partial inhibition of nitrocefin turnover at 1 μM and total abrogation at 10 μM (2b). The initial velocity (v i ) of the reaction between Bla Mab and nitrocefin was monitored for a range of substrate concentrations (1-500 μM) and relebactam concentrations (0, 0.5, 0.75, 1 and 2.5 μM). This data was plotted v i vs [S] in order to determine K m values (2c/f). The values for K obs were obtained as previously described ( Dubée et al., 2014 ) and plotted against relebactam concentrations ([I]) to deduce a carbamylation rate ( K 2 / K i ) for Bla Mab (2d). The kinetics of Bla Mab decarbamylation were assessed to show the recovery of nitrocefin hydrolysis by Bla Mab after inhibition by relebactam in order to derive a K off value (2e). Kinetic parameters were derived as described previously (2f) ( Dubée et al., 2014 ).

    Article Snippet: The hydrolysis of nitrocefin was monitored at 486 nm using a Multiskan Go plate reader (Thermo Scientific).

    Techniques: Inhibition, Thin Layer Chromatography, Activity Assay, Concentration Assay, Derivative Assay