Purification and characterization of membrane-bound chitin synthase.

@article{Machida1993PurificationAC,
  title={Purification and characterization of membrane-bound chitin synthase.},
  author={Sachiko Machida and Masaki Saito},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 3},
  pages={1702-7}
}
The membrane-bound chitin synthase, a key enzyme of chitin biosynthesis, was purified, for the first time to homogeneity as a zymogen form. Digitonin could solubilize the enzyme from microsomal fraction of the filamentous fungus Absidia glauca, with 60-70% of the enzyme activity. The solubilized form of the enzyme was effectively purified by a sequence of chelating Sepharose, concanavalin A-Sepharose, and Mono Q column. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the purified… CONTINUE READING