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Catalytic and DNA-Hydrolyzing Activities of Purified Immunoglobulins IgG from Patients Sera with Autoimmune Disease by Pseudobiospecific Chromatography Using Histidyl-Aminohexyl-Sepharose

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Abstract

Catalytic autoimmune antibodies from patients with antiphospholipid (aPL) antibodies were purified using histidyl-aminohexyl-sepharose gel. The sera were loaded on the columns equilibrated with 25 mM MOPS buffer pH 7.4 and the absorbed proteins were eluted by adding 0.2 M NaCl in the equilibrating buffer. Antibodies purity was evaluated by SDS-PAGE. The purified immunoglobulins G from patients with (aPL) sera by histidyl-aminohexyl-sepharose show DNA-degrading activity of the plasmid pUC19 DNA and catalytic activity in hydrolyzing the peptide substrate Pro-Phe-Arg-7-amido-4-methylcoumarin.

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Correspondence to A. Elkak.

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Elkak, A., Bourhim, M., Coffinier, Y. et al. Catalytic and DNA-Hydrolyzing Activities of Purified Immunoglobulins IgG from Patients Sera with Autoimmune Disease by Pseudobiospecific Chromatography Using Histidyl-Aminohexyl-Sepharose. Chromatographia 60, 165–169 (2004). https://doi.org/10.1365/s10337-004-0333-6

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  • DOI: https://doi.org/10.1365/s10337-004-0333-6

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