Solubilization and one-step purification of mannosylphosphodolichol synthase from Trichoderma reesei.

@article{Kruszewska1996SolubilizationAO,
  title={Solubilization and one-step purification of mannosylphosphodolichol synthase from Trichoderma reesei.},
  author={Joanna S. Kruszewska and Urszula Perlińska-Lenart and Grażyna Palamarczyk},
  journal={Acta biochimica Polonica},
  year={1996},
  volume={43 2},
  pages={397-401}
}
Mannosylphosphodolichol synthase (MPD-synthase) (EC 2.4.1.830) catalyzing formation of MPD from GDPMan and dolichylphosphate (PD) has been purified from T. reesei cellular membranes almost to homogeneity. Selective solubilization of the enzyme was followed by one step purification on Phenyl-Sepharose column. SDS/ PAGE of the purified enzyme fraction revealed the presence of a protein band of 31 kDa corresponding to the apparent molecular mass of the MPD-synthase purified from S. cerevisiae… CONTINUE READING