Human liver iduronate-2-sulphatase. Purification, characterization and catalytic properties.

@article{Bielicki1990HumanLI,
  title={Human liver iduronate-2-sulphatase. Purification, characterization and catalytic properties.},
  author={Julie Bielicki and Craig Freeman and Peter Roy Clements and John J. Hopwood},
  journal={The Biochemical journal},
  year={1990},
  volume={271 1},
  pages={75-86}
}
Human iduronate-2-sulphatase (EC 3.1.6.13), which is involved in the lysosomal degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate, was purified more than 500,000-fold in 5% yield from liver with a six-step column procedure, which consisted of a concanavalin A-Sepharose-Blue A-agarose coupled step, chromatofocusing, gel filtration on TSK HW 50S-Fractogel, hydrophobic separation on phenyl-Sepharose CL-4B and size separation on TSK G3000SW Ultrapac. Two major forms were… CONTINUE READING

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