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- W2026048218 abstract "Tetrahydrofolate dehydrogenase (5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3; formerly known as dihydrofolate reductase) from a high enzyme mutant of L1210 mouse leukemia was purified to homogeneity by a simple two step procedure involving pH 5.1 precipitation of inert protein, and affinity chromatography employing a methotrexate-agarose column. By raising the pH and ionic strength of the eluting buffer from 0.05 M citrate (pH 6.0) to 0.05 M Tris-HCl (pH 8.5) containing 0.1 M KCl, a peak was eluted containing pure enzyme (spec. act. 2800 μmoles/h per mg). Purity was confirmed by methotrexate titration and polyacrylamide disc electrophoresis. A second small peak containing tetrahydrofolate dehydrogenase activity was eluted by further increasing the pH of the 0.05 M Tris-HCl buffer to 9.0, and increasing the KCl concentration to 0.4 M. The material in this peak showed an absorbance at 258 nm, suggesting that a nucleotide was bound to the enzyme. The identify of this material has yet not been established." @default.
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- W2026048218 date "1972-04-01" @default.
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- W2026048218 title "Improved purification of tetrahydrofolate dehydrogenase from L1210 leukemia by affinity chromatography" @default.
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- W2026048218 doi "https://doi.org/10.1016/0005-2744(72)90193-3" @default.
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