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- W2019918829 abstract "Folate was coupled to AH-Sepharose 4B, the gel poured into small columns, and the Sepharose-bound folate reduced in situ to dihydrofolate by dithionite/ascorbate at pH 6 to 7. The dihydrofolate-Sepharose column was used to purify guanosine triphosphate cyclohydrolase I (EC 3.5.4.16) and dihydrofolate reductase (EC 1.5.1.3). All steps were carried out in the cold and in the presence of 20 mm mercaptoethanol. GTP cyclohydrolase I bound strongly to the dihydrofolate-Sepharose column and was purified several-hundred-fold in a single step. It did not bind to folate-Sepharose. Binding to dihydrofolate-Sepharose is assumed to reflect a physiological role of dihydrofolate. GTP cyclohydrolase II did not bind to either folate- or dihydrofolate-Sepharose. Dihydrofolate reductase from Escherichia coli B and from rat liver did not bind to folate-Sepharose under the test conditions, but could be well purified on the dihydrofolate-Sepharose column. This column is judged to beuseful for the purification of other folate-converting enzymes." @default.
- W2019918829 created "2016-06-24" @default.
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- W2019918829 date "1979-11-01" @default.
- W2019918829 modified "2023-10-16" @default.
- W2019918829 title "Purification of guanosine triphosphate cyclohydrolase I and dihydrofolate reductase on a dihydrofolate-sepharose affinity column" @default.
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- W2019918829 doi "https://doi.org/10.1016/0003-2697(79)90120-9" @default.
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