Publication
Aeromonas glycerophospholipid:cholesterol acyl transferase undergoes a conformational transition upon activation by treatment with trypsin. Chemical cross-linking and sedimentation velocity analysis showed that the lipase dimerizes due to removal of a region near its C-terminus. The lipase monomer has a sedimentation coefficient s20.w = 2.83 S, whereas the dimer has s20.w = 3.65 +/- 0.22 S. Hydrodynamic analysis using these sedimentation values and the masses determined by mass spectrometry indicated that the monomers are aligned side-by-side in the dimer. An important change occurs in the apparent partial specific volume of the molecule upon activation.
Yury Tsybin, Natalia Gasilova, Laure Menin, Anton Kozhinov, Konstantin Nagornov
Thomas Rizzo, Ahmed Ben Faleh, Stephan Warnke, Ali H Abikhodr, Teun Van Wieringen