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Fullerene–Interfaced Porphyrin Ligand in Affinity Chromatography of Membrane Proteins

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Abstract

To purify the mammalian cell membrane porphyrin binding proteins (PBP), an original affinity chromatographic technique is proposed. The method is based on the application of an agarose attached fullerene-porphyrin ligand connected to a polysaccharide gel matrix through the epoxy-cyclohexyl residue interface. A selective PBP-stationary phase coupling has been managed in a single column chromatographic run leading to a complete purification of the 17.6 kDa monomer protein from the rat myocardium mitochondria membranes. A synchronous pH and ionic strength linear gradients were used to separate this protein with a high specific affinity to the porphyrin K related structures from all non-specific sorption retained membrane proteins.

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Acknowledgment

This work was supported by the Iranian NanoTech Committee research grant QR200754/2005-08 and, in part, by the Russian Basic Research Foundation grant 10-OX(B)2005-06.

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Authors and Affiliations

  1. School of Pharmacy, I. M. Sechenov Moscow Medical Academy, Moscow, Russia

    Nima Amirshahi & Renad N. Alyautdin

  2. School of Medicine, Tehran University of Medical Sciences, Tehran, I. R. Iran

    S. Mahdi Rezayat & Saeed Sarkar

  3. Department of Chemistry, M. V. Lomonosov Moscow State University, Moscow, Russia

    Marina A. Orlova, Alexey P. Orlov & Andrey A. Poloznikov

  4. N. N. Semenov Institute for Chemical Physics, Russian Academy of Sciences, Moscow, Russia

    Dmitry A. Kuznetsov

Authors
  1. Nima Amirshahi
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  2. Renad N. Alyautdin
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  3. S. Mahdi Rezayat
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  4. Saeed Sarkar
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  5. Marina A. Orlova
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  6. Alexey P. Orlov
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  7. Andrey A. Poloznikov
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  8. Dmitry A. Kuznetsov
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Correspondence to Nima Amirshahi.

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Amirshahi, N., Alyautdin, R.N., Rezayat, S.M. et al. Fullerene–Interfaced Porphyrin Ligand in Affinity Chromatography of Membrane Proteins. Chroma 68, 295–298 (2008). https://doi.org/10.1365/s10337-008-0681-8

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  • DOI: https://doi.org/10.1365/s10337-008-0681-8

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