Studies on inactivation of lipoprotein lipase: role of the dimer to monomer dissociation.

@article{Osborne1985StudiesOI,
  title={Studies on inactivation of lipoprotein lipase: role of the dimer to monomer dissociation.},
  author={James Osborne and Gunilla Bengtsson-Olivecrona and Nan Sook Lee and Thomas Olivecrona},
  journal={Biochemistry},
  year={1985},
  volume={24 20},
  pages={5606-11}
}
Sedimentation equilibrium analysis demonstrated that preparations of bovine lipoprotein lipase contain a complex mixture of dimers and higher oligomers of enzyme protein. Enzyme activity profiles from sedimentation equilibrium as well as from gel filtration indicated that activity is associated almost exclusively with the dimer fraction. To explore if the enzyme could be dissociated into active monomers, 0.75 M guanidinium chloride was used. Sedimentation velocity measurements demonstrated that… CONTINUE READING

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