Effects of deletion of the carboxyl-terminal domain of ApoA-I or of its substitution with helices of ApoA-II on in vitro and in vivo lipoprotein association.

@article{Holvoet1996EffectsOD,
  title={Effects of deletion of the carboxyl-terminal domain of ApoA-I or of its substitution with helices of ApoA-II on in vitro and in vivo lipoprotein association.},
  author={Paul Holvoet and Zhenze Zhao and Els Deridder and A Dhoest and D{\'e}sir{\'e} Collen},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 32},
  pages={19395-401}
}
In the present study, the lipoprotein association of apoA-I, an apoA-I (DeltaAla190-Gln243) deletion mutant and an apoA-I (Asp1-Leu189)/apoA-II (Ser12-Gln77) chimera were compared. At equilibrium, 80% of the 125I-labeled apolipoproteins associated with lipoproteins in rabbit or human plasma but with very different distribution profiles. High density lipoprotein (HDL)2,3-associated fractions were 0.60 for apoA-I, 0.30 for the chimera, and 0.15 for the deletion mutant, and corresponding very high… CONTINUE READING

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