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• W2257325031 abstract "Dihydrofolate reductase has been purified from a methotrexate-resistant strain of Lactobacillus casei NCB 6375. By careful attention to growth conditions, up to 2.5 g of enzyme is obtained from a 400 litre culture. The purification procedure, involving poly-ethyleneimine treatment, DEAE-cellulose chromatography and affinity chromatography on methotrexate-aminohexyl-Sepharose, operates on the gram scale, with overall yields of 50-60%. Elution of the affinity column by reverse (upward) flow was used, as it led to recovery of the enzyme in a much smaller volume. The enzyme obtained appears to be more than 98% pure, as judged by gel electrophoresis, isoelectric focusing, and gel filtration. It has a mol.wt. of approx. 17900 and a turnover number of 4s-1 (50mM-triethanolamine/400mM-KCl, pH 7.2, 25 degrees C) with dihydrofolate and NADPH as substrates. The turnover number for folate is 0.02s-1. Michaelis constants for a variety of substrates have been measured by using a new fluorimetric assay (0.36 muM-dihydrofolate; 0.78 muM-NADPH), and binding constants determined by using the quenching of protein fluorescence (dihydrofolate, 2.25 X 10(6)M-1; NADPH, greater than 10(8)M-1). The pH/activity profile shows a single maximum at pH 7.3; at this pH, marked activation by 0.5M-NaCl is observed." @default.
• W2257325031 created "2016-06-24" @default.
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• W2257325031 date "1976-09-01" @default.
• W2257325031 modified "2023-10-18" @default.
• W2257325031 title "Large-scale purification and characterization of dihydrofolate reductase from a methotrexate-resistant strain of <i>Lactobacillus casei</i>" @default.
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• W2257325031 doi "https://doi.org/10.1042/bj1570559" @default.
• W2257325031 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1163897" @default.
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