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Purification of tetrahydrofolate dehydrogenase by affinity chromatography
Biochimica Et Biophysica Acta - Biomembranes, 1972Abstract Tetrahydrofolate dehydrogenase (5,6,7,8-tetrahydrofolate:NADP + oxidoreductase, EC 1.5.1.3; formerly known as dihydrofolate reductase) from a subline of the L1210 lymphoma has been purified to apparent homogeneity with high recovery by simple steps using agarose to which the enzyme inhibitor amethopterin was coupled. A crude (NH 4 ) 2 SO 4
B L Hillcoat
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Tetrahydrofolate dehydrogenase cytochemistry in acute lymphoblastic leukemia
European Journal of Haematology, 1988We studied the cytochemical distribution of tetrahydrofolate dehydrogenase (FH4D), an enzyme involved in nucleic acid metabolism and thus in cell proliferation and differentiation processes, in bone marrow blasts from 37 cases of acute lymphoblastic leukemia (ALL), of whom 23 were pediatric patients. 26 cases were analyzed at onset, 11 in relapse.
INVERNIZZI, ROSANGELA +6 more
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In Vitro Antimalarial Activity of Tetrahydrofolate Dehydrogenase Inhibitors
American Journal of Tropical Medicine and Hygiene, 1984Three tetrahydrofolate dehydrogenase (dihydrofolate reductase = EC 1.5.1.3) inhibitors were tested for antimalarial activity against Plasmodium falciparum, using an in vitro radioisotopic technique. Activity of each drug was tested in both normal RPMI medium 1640 and in modified medium (containing no p-aminobenzoic acid and 2.27 X 10(-8) M folic acid ...
Harrison C Spencer +2 more
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The recovery of liver tetrahydrofolate dehydrogenase activity from inhibition by methotrexate
Biochemical Pharmacology, 1969Abstract Rat liver tetrahydrofolate dehydrogenase activity in vivo recovers rapidly from inhibition by methotrexate, despite the known stability of the enzyme-inhibitor complex. Control levels of activity are usually regained within 24 hr following a single injection of methotrexate.
D C Williams
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Biochimica Et Biophysica Acta - Biomembranes, 1972
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 ...
P L Chello, A R Cashmore, J R Bertino
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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 ...
P L Chello, A R Cashmore, J R Bertino
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Archives of Microbiology, 2002
Recently, it has been shown that heterotrophic methylotrophic Proteobacteria contain tetrahydrofolate (H(4)F)- and tetrahydromethanopterin (H(4)MPT)-dependent enzymes. Here we report on the purification of two methylene tetrahydropterin dehydrogenases from the methylotroph Hyphomicrobium zavarzinii ZV580. Both dehydrogenases are composed of one type of
Julia A Vorholt +2 more
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Recently, it has been shown that heterotrophic methylotrophic Proteobacteria contain tetrahydrofolate (H(4)F)- and tetrahydromethanopterin (H(4)MPT)-dependent enzymes. Here we report on the purification of two methylene tetrahydropterin dehydrogenases from the methylotroph Hyphomicrobium zavarzinii ZV580. Both dehydrogenases are composed of one type of
Julia A Vorholt +2 more
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Archives of Biochemistry and Biophysics, 1999
10-Formyltetrahydrofolate dehydrogenase has previously been identified as a tight binding protein of the polyglutamate forms of tetrahydrofolate (R. J. Cook and C. Wagner, Biochemistry 21, 4427-4434, 1982). Each subunit contains two independently folded domains connected by a linking peptide.
V Schirch +2 more
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10-Formyltetrahydrofolate dehydrogenase has previously been identified as a tight binding protein of the polyglutamate forms of tetrahydrofolate (R. J. Cook and C. Wagner, Biochemistry 21, 4427-4434, 1982). Each subunit contains two independently folded domains connected by a linking peptide.
V Schirch +2 more
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Biochimica Et Biophysica Acta - General Subjects, 1973
Abstract The effects of sex hormones, glucocorticoids, folate and protein deprivation upon tetrahydrofolate dehydrogenase activity in mammalian tissues were studied. In male rats estradiol induced significant increase in the activity of jejunal tetrahydrofolate dehydrogenase but only a slight increase occurred in the jejenum of hormone-treated female
E F Smith, J R Bertino
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Abstract The effects of sex hormones, glucocorticoids, folate and protein deprivation upon tetrahydrofolate dehydrogenase activity in mammalian tissues were studied. In male rats estradiol induced significant increase in the activity of jejunal tetrahydrofolate dehydrogenase but only a slight increase occurred in the jejenum of hormone-treated female
E F Smith, J R Bertino
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Activation of tetrahydrofolate dehydrogenase by certain cations
Biochimica Et Biophysica Acta, 1962J R Bertino, J R Bertino
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A colorimetric assay system for tetrahydrofolate dehydrogenase
Biochemical Pharmacology, 1968D C Williams
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