Purification and characterization of a galactose-1-phosphate: UDP-glucose uridyltransferase from the red alga Galdieria sulphuraria.

@article{Gross1995PurificationAC,
  title={Purification and characterization of a galactose-1-phosphate: UDP-glucose uridyltransferase from the red alga Galdieria sulphuraria.},
  author={Wolfgang Gross and Claus Schnarrenberger},
  journal={European journal of biochemistry},
  year={1995},
  volume={234 1},
  pages={258-63}
}
The galactose-1-phosphate uridyltransferase of the red alga Galdieria sulphuraria has been purified about 1800-fold to a final specific activity of approximately 140 U/mg protein. The purification involved chromatography on DEAE-Fractogel, hydroxyapatite, decyl-agarose, and DEAE-Tentacle gel. After SDS/PAGE, the enzyme preparation showed only one protein band of 42 kDa. The enzyme is a homodimer with a molecular mass of 82 kDa as estimated from the sedimentation velocity or 60 kDa as estimated… CONTINUE READING
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