دورية أكاديمية
أعرض في EDS

Purification of secretory IgA monoclonal antibodies enriched fraction directly from cell culture medium using aqueous two-phase systems.

التفاصيل البيبلوغرافية
العنوان: Purification of secretory IgA monoclonal antibodies enriched fraction directly from cell culture medium using aqueous two-phase systems.
المؤلفون: Leite ACL; Biotechnology and Blood Products Laboratory, Department of Pharmaceutical Sciences, Federal University of Pernambuco, Avenida Artur de Sá, 50740-520 Recife, Pernambuco, Brazil. Electronic address: ana.lleite@ufpe.br., Nascimento TP; Federal Rural University of Pernambuco, Laboratory of Bioactive Products and Technology, Department of Morphology and Animal Physiology Animal, Av. Dom Manoel de Medeiros, s/n, 52171-900 Recife, Pernambuco, Brazil., da Cunha MNC; Federal University of Piauí, Campus Professor Cinobelina Elvas, 64900-000 Bom Jesus, Piauí, Brazil., Mehari Y; Department of Biotechnology, Institute of Bioprocess Science and Engineering, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria; Austrian Centre of Industrial Biotechnology [ACIB], Muthgasse 18, 1190 Vienna, Austria., Berger E; Department of Biotechnology, Institute of Bioprocess Science and Engineering, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria; Austrian Centre of Industrial Biotechnology [ACIB], Muthgasse 18, 1190 Vienna, Austria., Scheich D; Department of Biotechnology, Institute of Bioprocess Science and Engineering, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria; Austrian Centre of Industrial Biotechnology [ACIB], Muthgasse 18, 1190 Vienna, Austria., Lingg N; Department of Biotechnology, Institute of Bioprocess Science and Engineering, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria; Austrian Centre of Industrial Biotechnology [ACIB], Muthgasse 18, 1190 Vienna, Austria., Jungbauer A; Department of Biotechnology, Institute of Bioprocess Science and Engineering, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria; Austrian Centre of Industrial Biotechnology [ACIB], Muthgasse 18, 1190 Vienna, Austria. Electronic address: alois.jungbauer@boku.ac.at.
المصدر: International journal of biological macromolecules [Int J Biol Macromol] 2024 Aug; Vol. 275 (Pt 2), pp. 133581. Date of Electronic Publication: 2024 Jul 01.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
مواضيع طبية MeSH: Cricetulus* , Immunoglobulin A, Secretory*/chemistry , Antibodies, Monoclonal*/chemistry , Antibodies, Monoclonal*/isolation & purification , Polyethylene Glycols*/chemistry, Animals ; CHO Cells ; Culture Media/chemistry ; Hydrogen-Ion Concentration ; Cricetinae ; Water/chemistry
مستخلص: Secretory immunoglobulin A [sIgA] is a promising candidate for enteric therapeutics applications, and several sIgA-based constructs are currently being developed by groups utilizing clarified Chinese hamster ovary [CHO] cell culture supernatants. To the monoclonal antibody downstream processing typically entails chromatography-based purification processes beginning with Protein A chromatography. In this paper, aqueous two-phase systems [ATPS] were employed for the preliminary purification of secretory immunoglobulin A [sIgA] monoclonal antibody [mAb] from clarified CHO-cell culture supernatants. A 2 4 full factorial design was utilized. The influence of various process parameters such as pH, PEG molecular weight [M PEG ], PEG concentration [C PEG ], and phosphate salt concentration [C PHO ], on the sIgA partition coefficient [K sIgA] and the recovery index [Y] in the PEG phase were evaluated. The Elisa assay revealed that, in the ATPS conditions tested, sIgA mAb was mostly detected in PEG upper phase. Run 14 with the highest sIgA activity exhibited the following conditions: M PEG 8.000 g/mol, C PEG 12,5 %, pH 7,0 and C PHO 10 %, and a sIgA K of 94.50 and a recovery index [Y] of 33.52 %. The proposed platform provides straightforward implementation, yields comparable results, and offers significantly improved economics for manufacturing sIgA mAb biotherapeutics.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)
فهرسة مساهمة: Keywords: ATPS; Monoclonal antibodies; sIgA mAb
المشرفين على المادة: 0 (Immunoglobulin A, Secretory)
0 (Antibodies, Monoclonal)
3WJQ0SDW1A (Polyethylene Glycols)
0 (Culture Media)
059QF0KO0R (Water)
تواريخ الأحداث: Date Created: 20240703 Date Completed: 20240808 Latest Revision: 20240808
رمز التحديث: 20240808
DOI: 10.1016/j.ijbiomac.2024.133581
PMID: 38960262
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0003
DOI:10.1016/j.ijbiomac.2024.133581