دورية أكاديمية
Characterization of a recombinant monoclonal antibody by mass spectrometry combined with liquid chromatography.
| العنوان: | Characterization of a recombinant monoclonal antibody by mass spectrometry combined with liquid chromatography. |
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| المؤلفون: | Matamoros Fernández LE; Center of Molecular Immunology, Havana, Cuba., Kalume DE, Calvo L, Fernández Mallo M, Vallin A, Roepstorff P |
| المصدر: | Journal of chromatography. B, Biomedical sciences and applications [J Chromatogr B Biomed Sci Appl] 2001 Mar 10; Vol. 752 (2), pp. 247-61. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 9714109 Publication Model: Print Cited Medium: Print ISSN: 1387-2273 (Print) Linking ISSN: 13872273 NLM ISO Abbreviation: J Chromatogr B Biomed Sci Appl Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam ; New York : Elsevier, c1997-c2001. |
| مواضيع طبية MeSH: | Antibodies, Monoclonal/*chemistry , Chromatography, Liquid/*methods , Spectrometry, Mass, Electrospray Ionization/*methods , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/*methods, Amino Acid Sequence ; Antibodies, Monoclonal/isolation & purification ; Humans ; Molecular Sequence Data ; Peptide Mapping ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Trypsin/chemistry |
| مستخلص: | In this report, we present the characterization of a humanized monoclonal antibody specific for the human epidermal growth factor receptor (hEGFR). Direct analysis by matrix assisted laser desorption ionization mass spectrometry (MALDI-MS) of peptide mixtures and chromatographically isolated fractions allowed identification of 94.0% and 85.4% of the amino acid sequence of light and heavy chains, respectively. Microheterogeneity sources were identified in light and heavy chains and a previously unreported posttranslational modification for immunoglobulins was found. One N-glycosylation site was identified in the heavy chain with non-sialylated bianntenary fucosylated structures. This study is one of the first to assess the potential of MALDI-MS in combination with more conventional protein chemistry techniques for the characterization of monoclonal antibodies. |
| المشرفين على المادة: | 0 (Antibodies, Monoclonal) 0 (Recombinant Proteins) EC 3.4.21.4 (Trypsin) |
| تواريخ الأحداث: | Date Created: 20010329 Date Completed: 20010705 Latest Revision: 20190831 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/s0378-4347(00)00503-x |
| PMID: | 11270865 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1387-2273 |
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| DOI: | 10.1016/s0378-4347(00)00503-x |