Human liver methenyltetrahydrofolate synthetase: improved purification and increased affinity for folate polyglutamate substrates.

@article{Bertrand1987HumanLM,
  title={Human liver methenyltetrahydrofolate synthetase: improved purification and increased affinity for folate polyglutamate substrates.},
  author={Richard Bertrand and Robert E Mackenzie and Jacques Jolivet},
  journal={Biochimica et biophysica acta},
  year={1987},
  volume={911 2},
  pages={154-61}
}
Methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclodehydrase (cyclo-ligase) (ADP-forming) EC 6.3.3.2) catalyzes the ATP- and Mg2+-dependent transformation of 5-formyltetrahydrofolate (leucovorin) to 5,10-methenyltetrahydrofolate. The enzyme has been purified 49,000-fold from human liver by a two-column procedure with Blue Sepharose followed by folinate-Sepharose chromatography. It appears as a single band both on SDS-polyacrylamide gel electrophoresis (Mr 27,000) and on… CONTINUE READING