Head-to-tail and side-by-side oligomerization of human carbonic anhydrase II: a small angle X-ray scattering study

摘要: Solvent-induced directional aggregation of human carbonic anhydrase II (hCA) was studied by small angle X-ray scattering and fluorescence fourth-derivative ultraviolet absorption spectroscopy. We propose that hCA at 5 mg ml(-1) in pure water forms head-to-tail oligomers built up, on average, four to five monomers. At higher protein concentrations, the associate pair-wise side-by-side. Spectroscopic evidence suggests subunits forming aggregates are tightly folded, but with a structure differs, least locally, from native state. A more complex pattern observed under solvent conditions favor removal zinc enzyme-active site, which significantly less compact than water. may provide useful model investigate effects additives genetic manipulation aggregation.