Carboxyl-terminal domain truncation alters apolipoprotein A-I in vivo catabolism.

@article{Schmidt1995CarboxylterminalDT,
  title={Carboxyl-terminal domain truncation alters apolipoprotein A-I in vivo catabolism.},
  author={Hartmut H-J Schmidt and Alan T Remaley and John A. Stonik and Robert Ronan and Axel Wellmann and Fairwell Thomas and Loren A Zech and Hollis B Brewer and Jeffery M Hoeg},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 10},
  pages={5469-75}
}
Apolipoprotein A-I (apoA-I), the major protein of high density lipoproteins, facilitates reverse cholesterol transport from peripheral tissue to liver. To determine the structural motifs important for modulating the in vivo catabolism of human apoA-I (h-apoA-I), we generated carboxyl-terminal truncation mutants at residues 201 (apoA-I201), 217 (apoA-I217), and 226 (apoA-I226) by site-directed mutagenesis. ApoA-I was expressed in Escherichia coli as a fusion protein with the maltose binding… CONTINUE READING
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