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Findings from M. Al-Majdoub and Co-Authors Update Knowledge of Immunoglobulins (A novel strategy for the rapid preparation and isolation of intact...

August 19, 2014



Findings from M. Al-Majdoub and Co-Authors Update Knowledge of Immunoglobulins (A novel strategy for the rapid preparation and isolation of intact immune complexes from peptide mixtures)

By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Immunology. According to news originating from Cairo, Egypt, by NewsRx correspondents, research stated, "The development and application of a miniaturized affinity system for the preparation and release of intact immune complexes are demonstrated. Antibodies were reversibly affinity-adsorbed on pipette tips containing protein G' and protein A, respectively."

Our news journalists obtained a quote from the research, "Antigen proteins were digested with proteases and peptide mixtures were exposed to attached antibodies; forming antibody-epitope complexes, that is, immune complexes. Elution with millimolar indole propionic acid (IPA)-containing buffers under neutral pH conditions allowed to effectively isolate the intact immune complexes in purified form. Size exclusion chromatography was performed to determine the integrity of the antibody-epitope complexes. Mass spectrometric analysis identified the epitope peptides in the respective SEC fractions. His-tag-containing recombinant human glucose-6-phosphate isomerase in combination with an anti-His-tag monoclonal antibody was instrumental to develop the method. Application was extended to the isolation of the intact antibody-epitope complex of a recombinant human tripartite motif 21 (rhTRIM21) auto-antigen in combination with a rabbit polyclonal anti-TRIM21 antibody. Peptide chip analysis showed that antibody-epitope binding of rhTRIM21 peptide antibody complexes was not affected by the presence of IPA in the elution buffer. By contrast, protein G' showed an ion charge structure by electrospray mass spectrometry that resembled a denatured conformation when exposed to IPA-containing buffers."

According to the news editors, the research concluded: "The advantages of this novel isolation strategy are low sample consumption and short experimental duration in addition to the direct and robust methodology that provides easy access to intact antibody-antigen complexes under neutral pH and low salt conditions for subsequent investigations."

For more information on this research see: A novel strategy for the rapid preparation and isolation of intact immune complexes from peptide mixtures. Journal of Molecular Recognition, 2014;27(9):566-574. Journal of Molecular Recognition can be contacted at: Wiley-Blackwell, 111 River St, Hoboken 07030-5774, NJ, USA. (Wiley-Blackwell - www.wiley.com/; Journal of Molecular Recognition - onlinelibrary.wiley.com/journal/10.1002/(ISSN)1099-1352)

The news correspondents report that additional information may be obtained from M. Al-Majdoub, British Univ Egypt, Microbiol & Immunol Fac Pharm, Cairo, Egypt. Additional authors for this research include K.F.M. Opuni, Y. Yefremova, C. Koy, P. Lorenz, R.F. El-Kased, H.J. Thiesen and M.O. Glocker (see also Immunology).

Keywords for this news article include: Antibodies, Cairo, Egypt, Africa, Immunology, Blood Proteins, Immunoglobulins

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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