Argininosuccinate lyase: purification and characterization from human liver.

@article{OBrien1981ArgininosuccinateLP,
  title={Argininosuccinate lyase: purification and characterization from human liver.},
  author={W. O'Brien and Richard H. Barr},
  journal={Biochemistry},
  year={1981},
  volume={20 7},
  pages={
          2056-60
        }
}
Argininosuccinate lyase has been purified to near homogeneity and partially characterized from extracts of human liver. The purified enzyme had a specific activity of 10.3 mumol min-1 mg-1 in the forward, argininosuccinate cleaving, reaction and 8.0 mumol min-1 mg-1 in the reverse reaction. On the basis of electrophoretic mobility in sodium dodecyl sulfate containing polyacrylamide gels, the protein had a minimum molecular weight of 49 000. Sedimentation equilibrium centrifugation revealed a… CONTINUE READING

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