Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry
A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heter...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2016-03-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340915003261 |
| _version_ | 1818482685316694016 |
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| author | Bao Quoc Tran Christopher Barton Jinhua Feng Aimee Sandjong Sung Hwan Yoon Shivangi Awasthi Tao Liang Mohd M. Khan David P.A. Kilgour David R. Goodlett Young Ah Goo |
| author_facet | Bao Quoc Tran Christopher Barton Jinhua Feng Aimee Sandjong Sung Hwan Yoon Shivangi Awasthi Tao Liang Mohd M. Khan David P.A. Kilgour David R. Goodlett Young Ah Goo |
| author_sort | Bao Quoc Tran |
| collection | DOAJ |
| description | A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heterogeneity of glycosylated protein species. Specifically, glycan structure, sites, relative abundance levels, and termini structural conformation were investigated by use of Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) linked to an Orbitrap. Incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme Streptococcus pyogenes (IdeS) with MALDI-ISD analysis extended sequence coverage of the internal region of the proteins without pre-fractionation. The data in this article is associated with the research article published in Journal of Proteomics (Tran et al., 2015) [1]. |
| first_indexed | 2024-12-10T11:50:34Z |
| format | Article |
| id | doaj.art-2777dc54923b46ecb5fa970fc176846d |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-10T11:50:34Z |
| publishDate | 2016-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-2777dc54923b46ecb5fa970fc176846d2022-12-22T01:49:57ZengElsevierData in Brief2352-34092016-03-0166876Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometryBao Quoc Tran0Christopher Barton1Jinhua Feng2Aimee Sandjong3Sung Hwan Yoon4Shivangi Awasthi5Tao Liang6Mohd M. Khan7David P.A. Kilgour8David R. Goodlett9Young Ah Goo10Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USAMedImmune, LLC, Gaithersburg, MD, USAMedImmune, LLC, Gaithersburg, MD, USAMedImmune, LLC, Gaithersburg, MD, USADepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USADepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USADepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USADepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USADepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USADepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USA; Corresponding authors.Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USA; Corresponding authors.A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heterogeneity of glycosylated protein species. Specifically, glycan structure, sites, relative abundance levels, and termini structural conformation were investigated by use of Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) linked to an Orbitrap. Incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme Streptococcus pyogenes (IdeS) with MALDI-ISD analysis extended sequence coverage of the internal region of the proteins without pre-fractionation. The data in this article is associated with the research article published in Journal of Proteomics (Tran et al., 2015) [1].http://www.sciencedirect.com/science/article/pii/S2352340915003261 |
| spellingShingle | Bao Quoc Tran Christopher Barton Jinhua Feng Aimee Sandjong Sung Hwan Yoon Shivangi Awasthi Tao Liang Mohd M. Khan David P.A. Kilgour David R. Goodlett Young Ah Goo Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry Data in Brief |
| title | Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry |
| title_full | Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry |
| title_fullStr | Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry |
| title_full_unstemmed | Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry |
| title_short | Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry |
| title_sort | glycosylation characterization of therapeutic mabs by top and middle down mass spectrometry |
| url | http://www.sciencedirect.com/science/article/pii/S2352340915003261 |
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