A Fullerene C₆₀-Based Ligand in a Stationary Phase
for Affine Chromatography
of Membrane Porphyrin-Binding Proteins

N. Amirshakhi^a, R. N. Alyautdin^a, A. P. Orlov^b, A. A. Poloznikov^b, and D. A. Kuznetsov^c

^a Sechenov Medical Academy, Moscow, Russia

e-mail: amupwaxu@gmail.com

^b Faculty of Chemistry, Moscow State University, Moscow, Russia

e-mail: orlova.radiochem@mail.ru

^c Semenov Institute of Chemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, Russia

e-mail: kuznetsov.icp@mail.ru

Received April 1, 2008

Abstract—A new affine chromatography technique is suggested for the purification of porphyrin-binding pro-
teins (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, synchro-
nous linear pH and ionic strength gradients were used.

DOI: 10.1134/S0036024408110277

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