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Physical and chemical characterization of the oligomerization state of the Aeromonas hydrophila lipase/acyltransferase
Author(s) -
Ausio Juan,
van der Goot F.Gisou,
Buckley J.Thomas
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80674-j
Subject(s) - lipase , dimer , chemistry , sedimentation coefficient , monomer , sedimentation equilibrium , partial specific volume , crystallography , molecule , stereochemistry , biochemistry , enzyme , organic chemistry , polymer
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 s 20,w = 2.83 S, whereas the dimer has s 20,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.