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Albani D, Parisi B, Carbonera D, et al. Dihydrofolate reductase from Daucus carota cell suspension cultures: purification, molecular and kinetic characterization. Plant Mol Biol. 1985;5(6):363-72doi: 10.1007/BF00037557.
Albani, D., Parisi, B., Carbonera, D., & Cella, R. (1985). Dihydrofolate reductase from Daucus carota cell suspension cultures: purification, molecular and kinetic characterization. Plant molecular biology, 5(6), 363-72. https://doi.org/10.1007/BF00037557
Albani, D, et al. "Dihydrofolate reductase from Daucus carota cell suspension cultures: purification, molecular and kinetic characterization." Plant molecular biology vol. 5,6 (1985): 363-72. doi: https://doi.org/10.1007/BF00037557
Albani D, Parisi B, Carbonera D, Cella R. Dihydrofolate reductase from Daucus carota cell suspension cultures: purification, molecular and kinetic characterization. Plant Mol Biol. 1985 Nov;5(6):363-72. doi: 10.1007/BF00037557. PMID: 24306990.
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Plant Mol Biol. 1985 Nov;5(6):363-72. doi: 10.1007/BF00037557.

Dihydrofolate reductase from Daucus carota cell suspension cultures: purification, molecular and kinetic characterization.

Plant molecular biology

D Albani, B Parisi, D Carbonera, R Cella

Affiliations

  1. Dipartimento di Genetica e Microbiologia, Via S. Epifanio, 14, 27100, Pavia, Italy.

PMID: 24306990 DOI: 10.1007/BF00037557

Abstract

The purification of dihydrofolate reductase (5, 6, 7, 8 tetrahydrofolate: NADP(+) oxidoreductase, E.C.: 1.5.1.3) from Daucus carota to apparent homogeneity, is described. The enzyme is a soluble protein with a molecular weight of 183 000±2 500, composed of identical subunits of 58 400±1 000. The enzyme is only weakly recognized by antibodies against human DHFR. The carrot DHFR is characterized by a pH optimum of 5.9, Km values for dihydrofolate and NADPH of 3.7 μM and 2.2 μM, respectively and a turnover number of 4 750 or 1 500 when referring to the 183 K form or the 58 K monomer, respectively. Molecular and kinetic properties are remarkably different from those reported for the soybean enzyme. Sensitivity to methotrexate is similar to that of bacterial and mammalian enzymes while sensitivity to trimethoprim and dihydrotriazine is intermediate between the two groups of organisms.

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