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Mass spectrometric characterization of the isoforms in Escherichia coli recombinant DNA-derived interferon alpha-2b

The isoforms Iso-2, Iso-3, and Iso-4 of Escherichia coli-derived recombinant human interferon alpha-2b (rhIFN α-2b), generated by posttranslational modifications of the protein during fermentation, present a major problem in terms of purification and the yield of the drug substance. We report here t... Full description

Journal Title: Analytical Biochemistry 2011, Vol.408(1), pp.105-117
Main Author: Liu, Yan-Hui
Other Authors: Wylie, David , Zhao, Jia , Cure, Raymond , Cutler, Collette , Cannon-Carlson, Susan , Yang, Xiaoyu , Nagabhushan, Tattanahalli L , Pramanik, Birendra N
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0003-2697 ; E-ISSN: 1096-0309 ; DOI: 10.1016/j.ab.2010.08.033
Link: http://dx.doi.org/10.1016/j.ab.2010.08.033
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recordid: elsevier_sdoi_10_1016_j_ab_2010_08_033
title: Mass spectrometric characterization of the isoforms in Escherichia coli recombinant DNA-derived interferon alpha-2b
format: Article
creator:
  • Liu, Yan-Hui
  • Wylie, David
  • Zhao, Jia
  • Cure, Raymond
  • Cutler, Collette
  • Cannon-Carlson, Susan
  • Yang, Xiaoyu
  • Nagabhushan, Tattanahalli L
  • Pramanik, Birendra N
subjects:
  • E. Coli-Derived Recombinant Human Interferon Α-2b and Isoforms
  • Pyruvic Acid Ketimine Derivative of N-Terminal Cysteine
  • S-Glutathionylated Cys98
  • Acetylated Cys1
  • LC/Esi–MS
  • LC/Esi–MS/MS
  • Esi–MS N
  • High-Resolution Ltq Orbitrap
  • Maldi–Tof–MS
  • E. Coli-Derived Recombinant Human Interferon Α-2b and Isoforms
  • Pyruvic Acid Ketimine Derivative of N-Terminal Cysteine
  • S-Glutathionylated Cys98
  • Acetylated Cys1
ispartof: Analytical Biochemistry, 2011, Vol.408(1), pp.105-117
description: The isoforms Iso-2, Iso-3, and Iso-4 of Escherichia coli-derived recombinant human interferon alpha-2b (rhIFN α-2b), generated by posttranslational modifications of the protein during fermentation, present a major problem in terms of purification and the yield of the drug substance. We report here the structural characterization of these isoforms by mass spectrometry (MS) methods. An extensive MS study was conducted on Iso-4, which is composed of up to 75% of the in-process IFN, and on the native rhIFN α-2b. The trypsin-digested peptide mixtures generated from the two samples were analyzed by liquid chromatography (LC)–MS, and targeted peptides were further studied by LC–tandem MS (triple quadrupole mass spectrometer), high-resolution MS n (LTQ Orbitrap), and matrix-assisted laser desorption/ionization MS (MALDI–MS). The structure of Iso-4 was elucidated as a novel pyruvic acid ketimine derivative of the N-terminal cysteine (Cys1) of IFN α-2b, where the disulfide...
language: eng
source:
identifier: ISSN: 0003-2697 ; E-ISSN: 1096-0309 ; DOI: 10.1016/j.ab.2010.08.033
fulltext: fulltext
issn:
  • 0003-2697
  • 00032697
  • 1096-0309
  • 10960309
url: Link


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titleMass spectrometric characterization of the isoforms in Escherichia coli recombinant DNA-derived interferon alpha-2b
creatorLiu, Yan-Hui ; Wylie, David ; Zhao, Jia ; Cure, Raymond ; Cutler, Collette ; Cannon-Carlson, Susan ; Yang, Xiaoyu ; Nagabhushan, Tattanahalli L ; Pramanik, Birendra N
ispartofAnalytical Biochemistry, 2011, Vol.408(1), pp.105-117
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subjectE. Coli-Derived Recombinant Human Interferon Α-2b and Isoforms ; Pyruvic Acid Ketimine Derivative of N-Terminal Cysteine ; S-Glutathionylated Cys98 ; Acetylated Cys1 ; LC/Esi–MS ; LC/Esi–MS/MS ; Esi–MS N ; High-Resolution Ltq Orbitrap ; Maldi–Tof–MS ; E. Coli-Derived Recombinant Human Interferon Α-2b and Isoforms ; Pyruvic Acid Ketimine Derivative of N-Terminal Cysteine ; S-Glutathionylated Cys98 ; Acetylated Cys1
descriptionThe isoforms Iso-2, Iso-3, and Iso-4 of Escherichia coli-derived recombinant human interferon alpha-2b (rhIFN α-2b), generated by posttranslational modifications of the protein during fermentation, present a major problem in terms of purification and the yield of the drug substance. We report here the structural characterization of these isoforms by mass spectrometry (MS) methods. An extensive MS study was conducted on Iso-4, which is composed of up to 75% of the in-process IFN, and on the native rhIFN α-2b. The trypsin-digested peptide mixtures generated from the two samples were analyzed by liquid chromatography (LC)–MS, and targeted peptides were further studied by LC–tandem MS (triple quadrupole mass spectrometer), high-resolution MS n (LTQ Orbitrap), and matrix-assisted laser desorption/ionization MS (MALDI–MS). The structure of Iso-4 was elucidated as a novel pyruvic acid ketimine derivative of the N-terminal cysteine (Cys1) of IFN α-2b, where the disulfide...
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The isoforms Iso-2, Iso-3, and Iso-4 of Escherichia coli-derived recombinant human interferon alpha-2b (rhIFN α-2b), generated by posttranslational modifications of the protein during fermentation, present a major problem in terms of purification and the yield of the drug substance. We report here the structural characterization of these isoforms by mass spectrometry (MS) methods. An extensive MS study was conducted on Iso-4, which is composed of up to 75% of the in-process IFN, and on the native rhIFN α-2b. The trypsin-digested peptide mixtures generated from the two samples were analyzed by liquid chromatography (LC)–MS, and targeted peptides were further studied by LC–tandem MS (triple quadrupole mass spectrometer), high-resolution MS n (LTQ Orbitrap), and matrix-assisted laser desorption/ionization MS (MALDI–MS). The structure of Iso-4 was elucidated as a novel pyruvic acid ketimine derivative of the N-terminal cysteine (Cys1) of IFN α-2b, where the disulfide...

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abstract

The isoforms Iso-2, Iso-3, and Iso-4 of Escherichia coli-derived recombinant human interferon alpha-2b (rhIFN α-2b), generated by posttranslational modifications of the protein during fermentation, present a major problem in terms of purification and the yield of the drug substance. We report here the structural characterization of these isoforms by mass spectrometry (MS) methods. An extensive MS study was conducted on Iso-4, which is composed of up to 75% of the in-process IFN, and on the native rhIFN α-2b. The trypsin-digested peptide mixtures generated from the two samples were analyzed by liquid chromatography (LC)–MS, and targeted peptides were further studied by LC–tandem MS (triple quadrupole mass spectrometer), high-resolution MS n (LTQ Orbitrap), and matrix-assisted laser desorption/ionization MS (MALDI–MS). The structure of Iso-4 was elucidated as a novel pyruvic acid ketimine derivative of the N-terminal cysteine (Cys1) of IFN α-2b, where the disulfide...

pubElsevier Inc
doi10.1016/j.ab.2010.08.033
lad01Analytical Biochemistry
date2011-01-01