High-performance liquid affinity chromatography on silica-bound alcohol dehydrogenase.

@article{Nilsson1983HighperformanceLA,
  title={High-performance liquid affinity chromatography on silica-bound alcohol dehydrogenase.},
  author={Kerstin Nilsson and P. O. Larsson},
  journal={Analytical biochemistry},
  year={1983},
  volume={134 1},
  pages={60-72}
}
Horse liver alcohol dehydrogenase was immobilized on glycerylpropyl-silica (10 micron, 1000-A pores) activated with 2,2,2-trifluoroethanesulfonyl chloride (tresyl chloride). The coupling and activity yield was almost 100%. The coenzyme-binding sites were equivalent and virtually unaffected by the immobilization process, as judged from Scatchard plots and active-site titrations. The silica-bound enzyme, packed in steel columns, was integrated with HPLC equipment and then successfully used for… CONTINUE READING