Purification of delta-aminolevulinate dehydratase from genetically engineered yeast.

@article{Borralho1990PurificationOD,
  title={Purification of delta-aminolevulinate dehydratase from genetically engineered yeast.},
  author={L M Borralho and C H Ortiz and Anita Dolly Panek and James R. Mattoon},
  journal={Yeast},
  year={1990},
  volume={6 4},
  pages={319-30}
}
Saccharomyces cerevisiae transformed with a multicopy plasmid carrying the yeast structural gene HEM2, which codes for delta-aminolevulinate dehydratase, was enriched 20-fold in the enzyme. Beginning with cell-free extracts of transformed cells, the dehydratase was purified 193-fold to near-homogeneity. This represents a 3900-fold purification relative to the enzyme activity in normal, untransformed yeast cells. The specific activity of the purified enzyme was 16.2 mumol h-1 per mg protein at… CONTINUE READING