Mechanism of cholesteryl ester transfer protein inhibition by a neutralizing monoclonal antibody and mapping of the monoclonal antibody epitope.

@article{Swenson1989MechanismOC,
  title={Mechanism of cholesteryl ester transfer protein inhibition by a neutralizing monoclonal antibody and mapping of the monoclonal antibody epitope.},
  author={T. Swenson and C. Hesler and M. L. Brown and E. Quinet and P. Trotta and M. Haslanger and F. C. Gaeta and Y. Marcel and R. Milne and A. Tall},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 24},
  pages={
          14318-26
        }
}
The plasma cholesteryl ester transfer protein (CETP, Mr 74,000) has a binding site for neutral lipid which can readily equilibrate with lipoprotein cholesteryl esters or triglycerides. Recently, a monoclonal antibody (TP2) was obtained which neutralizes the cholesteryl ester (CE) and triglyceride (TG) transfer activities of the CETP. In this report, the epitope of the inhibitory monoclonal antibody has been localized to a hydrophobic 26-amino acid sequence at the COOH terminus of CETP. The Fab… Expand
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