Affinity chromatography of lysyl hydroxylase on concanavalin A-agarose.

@article{Turpeenniemi1977AffinityCO,
  title={Affinity chromatography of lysyl hydroxylase on concanavalin A-agarose.},
  author={T M Turpeenniemi and Ulla S Puistola and Henrik Anttinen and Kiri I. Kivirikko},
  journal={Biochimica et biophysica acta},
  year={1977},
  volume={483 1},
  pages={215-9}
}
Lysyl hydroxylase (peptidyllysine, 2-oxoglutarate: oxygen 5-oxidoreductase, EC 1.14.11.4) has a high affinity for columns of concanavalin A-agarose, which was markedly reduced in the presence of alpha-methyl-D-mannoside, suggesting that the enzyme is a glycoprotein. Once bound, the enzyme could not be eluted with the glycoside alone, whereas an effective elution was achieved by a combination of alpha-methyl-D-mannoside and ethylene glycol. The data thus suggest that hydrophobic interaction… CONTINUE READING