Structural domains of human apolipoprotein B-100. Differential accessibility to limited proteolysis of B-100 in low density and very low density lipoproteins.

@article{Chen1989StructuralDO,
  title={Structural domains of human apolipoprotein B-100. Differential accessibility to limited proteolysis of B-100 in low density and very low density lipoproteins.},
  author={Grace C. C. Chen and Shunyi Zhu and David A. Hardman and James W. Schilling and K F Lau and John P. Kane},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 24},
  pages={14369-75}
}
The structural domains of human apolipoprotein B-100 in low density lipoproteins (LDL) and the conformational changes of B-100 that accompany the conversion of very low density lipoproteins (VLDL) to LDL were investigated by limited proteolysis with 12 endoproteases of various specificities, and their cleavage sites were determined. In B-100 of LDL, we… CONTINUE READING