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Shimadzu Corporation electrospray ionization esi mode
Determination of reduction potentials of cSelS and cSelS U188C in GSH/GSSG redox buffers. The ratio of reduced and oxidized protein was determined by <t>electrospray</t> ionization mass spectroscopy. (A) A representative electrospray ionization mass spectrum of cSelS following incubation in a redox buffer poised at −232 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 680 to 870. (B) Deconvoluted spectrum. Molecular weights: alkylated cSelS 188Δ 15149 Da, oxidized cSelS 15300 Da and alkylated cSelS 15414 Da. (C) A representative electrospray ionization mass spectrum of cSelS U188C following incubation in a redox buffer poised at −209 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 685 to 870. (D) Deconvoluted spectrum. Molecular weights: oxidized cSelS U188C 15253 Da and alkylated cSelS U188C 15365 Da. Panels E and F display the resulting titration curves for (E) cSelS, reduction potential −234±1 mV; and (F) cSelS U188C, reduction potential −211±1 mV. The fraction of reduced protein is plotted against the buffer redox potential poised by the ratio of GSH to GSSG. The error bars represent the range of measurements (that is, highest and lowest values) among three repetitions, using two independent protein preparations.
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Article Title: The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro

Journal: Biochemistry

doi: 10.1021/bi4001358

Determination of reduction potentials of cSelS and cSelS U188C in GSH/GSSG redox buffers. The ratio of reduced and oxidized protein was determined by electrospray ionization mass spectroscopy. (A) A representative electrospray ionization mass spectrum of cSelS following incubation in a redox buffer poised at −232 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 680 to 870. (B) Deconvoluted spectrum. Molecular weights: alkylated cSelS 188Δ 15149 Da, oxidized cSelS 15300 Da and alkylated cSelS 15414 Da. (C) A representative electrospray ionization mass spectrum of cSelS U188C following incubation in a redox buffer poised at −209 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 685 to 870. (D) Deconvoluted spectrum. Molecular weights: oxidized cSelS U188C 15253 Da and alkylated cSelS U188C 15365 Da. Panels E and F display the resulting titration curves for (E) cSelS, reduction potential −234±1 mV; and (F) cSelS U188C, reduction potential −211±1 mV. The fraction of reduced protein is plotted against the buffer redox potential poised by the ratio of GSH to GSSG. The error bars represent the range of measurements (that is, highest and lowest values) among three repetitions, using two independent protein preparations.
Figure Legend Snippet: Determination of reduction potentials of cSelS and cSelS U188C in GSH/GSSG redox buffers. The ratio of reduced and oxidized protein was determined by electrospray ionization mass spectroscopy. (A) A representative electrospray ionization mass spectrum of cSelS following incubation in a redox buffer poised at −232 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 680 to 870. (B) Deconvoluted spectrum. Molecular weights: alkylated cSelS 188Δ 15149 Da, oxidized cSelS 15300 Da and alkylated cSelS 15414 Da. (C) A representative electrospray ionization mass spectrum of cSelS U188C following incubation in a redox buffer poised at −209 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 685 to 870. (D) Deconvoluted spectrum. Molecular weights: oxidized cSelS U188C 15253 Da and alkylated cSelS U188C 15365 Da. Panels E and F display the resulting titration curves for (E) cSelS, reduction potential −234±1 mV; and (F) cSelS U188C, reduction potential −211±1 mV. The fraction of reduced protein is plotted against the buffer redox potential poised by the ratio of GSH to GSSG. The error bars represent the range of measurements (that is, highest and lowest values) among three repetitions, using two independent protein preparations.

Techniques Used: Mass Spectrometry, Incubation, Titration

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    Shimadzu Corporation electrospray ionization esi mode
    Determination of reduction potentials of cSelS and cSelS U188C in GSH/GSSG redox buffers. The ratio of reduced and oxidized protein was determined by <t>electrospray</t> ionization mass spectroscopy. (A) A representative electrospray ionization mass spectrum of cSelS following incubation in a redox buffer poised at −232 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 680 to 870. (B) Deconvoluted spectrum. Molecular weights: alkylated cSelS 188Δ 15149 Da, oxidized cSelS 15300 Da and alkylated cSelS 15414 Da. (C) A representative electrospray ionization mass spectrum of cSelS U188C following incubation in a redox buffer poised at −209 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 685 to 870. (D) Deconvoluted spectrum. Molecular weights: oxidized cSelS U188C 15253 Da and alkylated cSelS U188C 15365 Da. Panels E and F display the resulting titration curves for (E) cSelS, reduction potential −234±1 mV; and (F) cSelS U188C, reduction potential −211±1 mV. The fraction of reduced protein is plotted against the buffer redox potential poised by the ratio of GSH to GSSG. The error bars represent the range of measurements (that is, highest and lowest values) among three repetitions, using two independent protein preparations.
    Electrospray Ionization Esi Mode, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/electrospray ionization esi mode/product/Shimadzu Corporation
    Average 90 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    electrospray ionization esi mode - by Bioz Stars, 2020-09
    90/100 stars
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    Determination of reduction potentials of cSelS and cSelS U188C in GSH/GSSG redox buffers. The ratio of reduced and oxidized protein was determined by electrospray ionization mass spectroscopy. (A) A representative electrospray ionization mass spectrum of cSelS following incubation in a redox buffer poised at −232 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 680 to 870. (B) Deconvoluted spectrum. Molecular weights: alkylated cSelS 188Δ 15149 Da, oxidized cSelS 15300 Da and alkylated cSelS 15414 Da. (C) A representative electrospray ionization mass spectrum of cSelS U188C following incubation in a redox buffer poised at −209 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 685 to 870. (D) Deconvoluted spectrum. Molecular weights: oxidized cSelS U188C 15253 Da and alkylated cSelS U188C 15365 Da. Panels E and F display the resulting titration curves for (E) cSelS, reduction potential −234±1 mV; and (F) cSelS U188C, reduction potential −211±1 mV. The fraction of reduced protein is plotted against the buffer redox potential poised by the ratio of GSH to GSSG. The error bars represent the range of measurements (that is, highest and lowest values) among three repetitions, using two independent protein preparations.

    Journal: Biochemistry

    Article Title: The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro

    doi: 10.1021/bi4001358

    Figure Lengend Snippet: Determination of reduction potentials of cSelS and cSelS U188C in GSH/GSSG redox buffers. The ratio of reduced and oxidized protein was determined by electrospray ionization mass spectroscopy. (A) A representative electrospray ionization mass spectrum of cSelS following incubation in a redox buffer poised at −232 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 680 to 870. (B) Deconvoluted spectrum. Molecular weights: alkylated cSelS 188Δ 15149 Da, oxidized cSelS 15300 Da and alkylated cSelS 15414 Da. (C) A representative electrospray ionization mass spectrum of cSelS U188C following incubation in a redox buffer poised at −209 mV and subsequent alkylation. The panel shows the charge state distribution of multiply charged ions [M+18H] 18+ to [M+22H] 22+ from m/z 685 to 870. (D) Deconvoluted spectrum. Molecular weights: oxidized cSelS U188C 15253 Da and alkylated cSelS U188C 15365 Da. Panels E and F display the resulting titration curves for (E) cSelS, reduction potential −234±1 mV; and (F) cSelS U188C, reduction potential −211±1 mV. The fraction of reduced protein is plotted against the buffer redox potential poised by the ratio of GSH to GSSG. The error bars represent the range of measurements (that is, highest and lowest values) among three repetitions, using two independent protein preparations.

    Article Snippet: Mass spectra were obtained using a QTOF Ultima (Waters, MA), operating under positive electrospray ionization (+ESI) mode, connected to an LC-20AD (Shimadzu, Kyoto, Japan).

    Techniques: Mass Spectrometry, Incubation, Titration