Abstract
DIHYDROFOLATE reductase (DHFR) is a NADPH-requiring enzyme, and as isolated from a methotrexate-resistant strain of E. coli B1,2, has two binding sites for NADPH3. The sequence of DHFR (Fig. 1) has been determined recently in our laboratory by standard methods including CNBr cleavage, enzymatic digestion, and manual Edman degradation with direct determination of the phenylthiohydantoins by gas chromatography and thin-layer chromatography. Novel methods used included free flow electrophoresis instead of ion exchange chromatography for the separation of peptides from tryptic digestion, and cellulose acetate electrophoresis to monitor separations of the peptides produced by CNBr. Details of this work will be reported elsewhere (C. D. B., J. A. Rodkey and J. M. Sondey, manuscript in preparation).
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BENNETT, C. Similarity in the Sequence of Escherichia coli Dihydrofolate Reductase with Other Pyridine Nucleotide-requiring Enzymes. Nature 248, 67–68 (1974). https://doi.org/10.1038/248067a0
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DOI: https://doi.org/10.1038/248067a0
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