Salt-independent binding of antibodies from human serum to thiophilic heterocyclic ligands |
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| Authors: | GH Scholz P Wippich S Leistner K Huse |
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| Institution: | aDepartment of Internal Medicine III, University of Leipzig, Philipp-Rosenthal-Strasse 27, D-04103 Leipzig, Germany;bInstitute of Pharmacy, Department of Pharmaceutical Chemistry, University of Leipzig, Leipzig, Germany |
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| Abstract: | Several thiophilic adsorbents with mercaptoheterocyclic ligands have been analyzed for their ability to bind human serum proteins in a salt-independent way. In contrast to 2-mercaptopyrimidine, 2-mercaptopyridine derived ligands show a group-selective binding of immunoglobulins and α2-macroglobulin, not only in the presence of high concentrations of sodium sulphate but in buffers with low ionic strength. The binding is restricted to thiophilic gels obtained by coupling 2-mercaptopyridine to a vinylsulphone-activated matrix and is not achieved on epichlorohydrin-activated gels. A novel thiophilic ligand based on mercaptonicotinic acid, containing a carboxylic group together with the thiophilic pattern of thioaromatic adsorbents, is demonstrated to be useful as an alternative purification scheme for antibodies. |
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| Keywords: | Proteins 2-Mercaptopyridine 2-Mercaptopyrimidine |
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