Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.

@article{Peterson1992HumanLL,
  title={Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.},
  author={Josi Peterson and Wilfred Y. Fujimoto and John D. Brunzell},
  journal={Journal of lipid research},
  year={1992},
  volume={33 8},
  pages={1165-70}
}
The objective of this study was to investigate how a conformational change in lipoprotein lipase (LPL) affects its molecular functions. Monoclonal antibodies (MAbs) were raised against purified bovine milk lipoprotein lipase. MAb 5D2 bound to human and bovine LPL both before and after denaturation of LPL. MAb 5F9 also recognized LPL from both species, but only after denaturation of the antigen, suggesting that a conformational change led to exposure of a previously hidden epitope. The MAbs were… CONTINUE READING