Plant triose phosphate isomerase isozymes : purification, immunological and structural characterization, and partial amino Acid sequences.

@article{Pichersky1984PlantTP,
  title={Plant triose phosphate isomerase isozymes : purification, immunological and structural characterization, and partial amino Acid sequences.},
  author={Eran Pichersky and Leslie D. Gottlieb},
  journal={Plant physiology},
  year={1984},
  volume={74 2},
  pages={340-7}
}
We report the first complete purifications of the cytosolic and plastid isozymes of triose phosphate isomerase (TPI; EC 5.3.1.1) from higher plants including spinach (Spinacia oleracea), lettuce (Lactuca sativa), and celery (Apium graveolens). Both isozymes are composed of two isosubunits with approximate molecular weight of 27,000; in spinach and lettuce the plastid isozyme is 200 to 400 larger than the cytosolic isozyme. The two isozymes, purified from lettuce, had closely similar amino acid… CONTINUE READING
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