Purification, crystallization and properties of triosephosphate isomerase from human skeletal muscle.

@article{Dbrowska1978PurificationCA,
  title={Purification, crystallization and properties of triosephosphate isomerase from human skeletal muscle.},
  author={Anna Dąbrowska and I Kamrowska and Tadeusz Baranowski},
  journal={Acta biochimica Polonica},
  year={1978},
  volume={25 3},
  pages={247-56}
}
1. Triosephosphate isomerase (D-glyceraldehyde-3-phosphate ketoisomerase, EC 5.3.1.1) from human skeletal muscle was purified to homogeneity and crystallized. The crystalline enzyme preparation was resolved on polyacrylamide-gel electrophoresis into three isoenzymes. 2. The molecular weight of the enzyme estimated by gel filtration method was found to be 57,400 +/- 3000. Molecular weight determination under dissociation conditions indicated a dimeric subunit structure of the enzyme. 3. The… CONTINUE READING