Chromatographia

, Volume 60, Issue 3–4, pp 165–169 | Cite as

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

  • A. Elkak
  • M. Bourhim
  • Y. Coffinier
  • M. A. Vijayalakshmi
Article

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.

Keywords

Column liquid chromatography Pseudobioaffinity chromatography Histidine-aminohexyl-sepharose gel Autoimmune diseases DNA-hydrolysis 

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Copyright information

© Friedr. Vieweg&Sohn Verlagsgesellschaft mbH 2004

Authors and Affiliations

  • A. Elkak
    • 1
    • 2
  • M. Bourhim
    • 3
  • Y. Coffinier
    • 3
  • M. A. Vijayalakshmi
    • 3
  1. 1.Department of Medical BiologyFaculty of Pharmacy, Lebanese UniversityBeirutLebanon
  2. 2.The National Council for Scientific ResearchBeirutLebanon
  3. 3.Laboratoire d’Interactions Moléculaires et de Technologie des séparationsUniversité de Technologie de CompiègneCompiègneFrance

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