کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
3443 171 2013 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Affinity chromatographic purification of human immunoglobulin M from human B lymphocyte cell culture supernatant
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Affinity chromatographic purification of human immunoglobulin M from human B lymphocyte cell culture supernatant
چکیده انگلیسی

Compared to immunoglobulin G purification with extensively studied affinity ligands such as protein A and protein G, little work has been done on affinity chromatographic purification of immunoglobulin M. Hexamer peptide ligand HWRGWV, previously shown to bind specifically to the Fc fragment of IgG, also demonstrated potential for IgM purification. This study presents further characterization and investigation of this ligand for its potential for purification of IgM. Different running conditions were employed in order to improve the recovery and purity of IgM. The final recovery and purity of the antibody is feedstock dependent, but can reach levels of both recovery and purity as high as 95%. The dependence of the recovery and purity on total loading amount and initial IgM concentration were investigated and discussed. Although relatively low dynamic binding capacities (DBC) in the range of 4.6–13.1 mg IgM/mL resin at linear flow rates from 173 to 35 cm/h were obtained for IgM compared to IgG because of the large molecular weight of IgM, the DBC value of HWRGWV for IgM is much greater than protein-based IgM affinity ligands found in the literature and is competitive with current commercially available affinity ligands, such as KAPTIVE-M, CaptureSelect IgM and Ultralink Immobilized Mannan Binding Protein.


► HWRGWV demonstrates great potential for affinity purification of hIgM.
► DBC for hIgM with HWRGWV is highly dependent on linear flow rate.
► Final recovery and purity for hIgM purification is feedstock dependent.
► As high as 95% for both recovery and purity can be achieved for hIgM purification.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical Engineering Journal - Volume 70, 15 January 2013, Pages 63–70
نویسندگان
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