Functional analyses of human apolipoprotein CII by site-directed mutagenesis: identification of residues important for activation of lipoprotein lipase.

@article{Shen2002FunctionalAO,
  title={Functional analyses of human apolipoprotein CII by site-directed mutagenesis: identification of residues important for activation of lipoprotein lipase.},
  author={Yan Shen and Aivar L{\~o}okene and Solveig Nilsson and Gunilla Olivecrona},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 6},
  pages={
          4334-42
        }
}
Apolipoprotein CII (apoCII) activates lipoprotein lipase (LPL). Seven residues, located on one face of a model alpha-helix spanning residues 59-75, are fully conserved in apoCII from ten different animal species. We have mutated these residues one by one. Substitution of Ala(59) by glycine, or Thr(62) and Gly(65) by alanine did not change the activation, indicating that these residues are outside the LPL-binding site. Replacement of Tyr(63), Ile(66), Asp(69), or Gln(70) by alanine lowered the… CONTINUE READING
Highly Cited
This paper has 20 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

References

Publications referenced by this paper.

Antibodies, A Laboratory Manual, Cold Spring by gest on O cber 5, 2017 hp://w w w .jb.org/ D ow nladed from Running title: Apolipoprotein CII mutants

E. Harlow, D. Lane
1988
View 1 Excerpt