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for eukaryotic expression of large protein complexes have been issued this month by the American Society of Biochemistry andMolecular Biology (ASBMB), and they highlight some of the most common problems encountered in protein purification fromprokaryotic and eukaryotic systems. At the ASBMB annual meeting in Boston, Walter Moore, a biochemist at the Scripps
Research Institute in San Diego, Calif., gave a talk entitled, “Recombinant protein complex purification from Eukaryotes,” a
topic in which he has been “working for a long time,” he says. His work, with Michael Snyder, a protein biochemist andbiotechnology company founder at the University of Florida in Gainesville, was published in Biochemical Society Transactionsin 2010. The guidelines represent a culmination of Moore’s work since then, and the motivation for the article was to prepare asingle resource for those who deal with such large complexes, notes John R. Walker, a graduate student in chemistry andbiochemistry at the University of California, San Diego, who has consulted Moore in this context. “This has been a long-termeffort,” he says. “Michael [Snyder] and I have both been assisting people with large complex proteins for the last 10 years. It’s
important to have guidelines that are very specific in terms of what things to make sure you do, and what to avoid.” Walker
collaborated with Moore, Michal Sobol, a chemist at Scripps, and other colleagues to compile the protocols, which offer
suggestions for purifying and crystallizing protein complexes. advertisement In the eyes of the authors, there are two major
types of eukaryotic proteins, which they recognize as being the major source for the study of large complexes. One is theproteasome, and the other is ribosomes. Proteasomes, for instance, are large protein complexes that facilitate the destruction ofdamaged, superflu
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