Purification and some properties of sucrose phosphorylase from Leuconostoc mesenteroides.

@article{Koga1991PurificationAS,
  title={Purification and some properties of sucrose phosphorylase from Leuconostoc mesenteroides.},
  author={Toshihiko Koga and Kaori Nakamura and Yoshiko Shirokane and Kanta Mizusawa and Satoshi Kitao and Masanori Kikuchi},
  journal={Agricultural and biological chemistry},
  year={1991},
  volume={55 7},
  pages={1805-10}
}
Sucrose phosphorylase (EC 2.4.1.7) was purified to homogeneity from Leuconostoc mesenteroides cells with a specific activity of 173.8 units per mg protein by ammonium sulfate fractionation, anion exchange HPLC on TSKgel DEAE-5PW, and hydrophobic HPLC on TSKgel Ether-5PW. The purified enzyme was an acidic protein having an isoelectric point of pH 4.6 and s0(20),W of 4.34S. The molecular weight of this enzyme was estimated to be 56,400 by sedimentation equilibrium, 55,000 by SDS-polyacrylamide… CONTINUE READING

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