Physical and chemical characterization of the oligomerization state of the Aeromonas hydrophila lipase/acyltransferase

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.


Published in:
FEBS Lett, 333, 3, 296-300
Year:
1993
Keywords:
Note:
Department of Biochemistry and Microbiology, University of Victoria, BC, Canada.
Laboratories:




 Record created 2009-01-30, last modified 2018-09-13


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