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A fullerene C60-based ligand in a stationary phase for affine chromatography of membrane porphyrin-binding proteins

  • Biophysical Chemistry
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Abstract

A new affine chromatography technique is suggested for the purification of porphyrin-binding proteins (PBP) from mammal cell membranes. The procedure uses new fullerene-porphyrin ligands immobilized on agarose and bound to the polysaccharide matrix via the epoxycyclohexyl residue. A selective PBP stationary phase was used in a single-column chromatography run for the complete purification of a monomeric protein (17.6 kDa) from mitochondrial membranes of rat myocardium. This protein was characterized by high affinity for porphyrin-related structures. To separate it from other nonspecifically sorbed membrane proteins, synchronous linear pH and ionic strength gradients were used.

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Correspondence to N. Amirshakhi.

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Original Russian Text © N. Amirshakhi, R.N. Alyautdin, A.P. Orlov, A.A. Poloznikov, D.A. Kuznetsov, 2008, published in Zhurnal Fizicheskoi Khimii, 2008, Vol. 82, No. 11, pp. 2170–2175.

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Amirshakhi, N., Alyautdin, R.N., Orlov, A.P. et al. A fullerene C60-based ligand in a stationary phase for affine chromatography of membrane porphyrin-binding proteins. Russ. J. Phys. Chem. 82, 1952–1957 (2008). https://doi.org/10.1134/S0036024408110277

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  • DOI: https://doi.org/10.1134/S0036024408110277

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