Purification and characterization of dihydrofolate reductase from methotrexate-resistant human lymphoblastoid cells

Dihydrofolate reductase has been isolated from methotrexate-resistant WIL2 human lymphoblastoid cells. This subline produces ca. 150 times more enzyme than the parental drug-sensitive line. The reductase has been purified to homogeneity by methotrexate affinity chromatography, gel filtration, and pr...

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Veröffentlicht in:	Biochemistry (Easton) 1983-02, Vol.22 (3), p.633-639
Hauptverfasser:	Delcamp, Tavner J, Susten, Sandra S, Blankenship, Dale T, Freisheim, James H
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - analysis Cell Line Drug Resistance Humans Hydrogen-Ion Concentration Kinetics lymphoblastoid cells Lymphocytes - drug effects Lymphocytes - enzymology man Methotrexate - pharmacology Potassium Chloride - pharmacology tetrahydrofolate dehydrogenase Tetrahydrofolate Dehydrogenase - isolation & purification Tetrahydrofolate Dehydrogenase - metabolism
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