Isolation of N5N10-Methylene Tetrahydrofolate Reductase From Bovine Brain
- 1 January 1972
- journal article
- research article
- Published by Taylor & Francis in Preparative Biochemistry
- Vol. 2 (3) , 207-214
- https://doi.org/10.1080/00327487208061471
Abstract
N5,N10 -methylene tetrahydrofolate reductase has been purified 100-fold from bovine brain. The initial fractionation with protamine sulfate and ammonium sulfate was followed by chromatography on DEAE-polyacrylamide gel (Bio Gel DM-30) and Sephadex G-200 as well as the selective adsorption and elution of the enzyme on calcium phosphate gel. The purified enzyme required FADH2 and catalyzed the reduction of the methylene group of N5,N10 -methylene tetrahydrofolate to the methyl group of N5 -methyl tetrahydrofolate. The pH optimum of the bovine brain reductase occurred at a pK of 6.5. The enzyme proved quite unstable. Both air oxidation and prolonged periods of storage at -20° inactivated the enzyme.Keywords
This publication has 10 references indexed in Scilit:
- Methionine synthesis by extracts of Salmonella typhimuriumBiochemical Journal, 1966
- Enzymatic Synthesis of the Methyl Group of MethioninePublished by Elsevier ,1965
- Naturally Occurring Forms of Folic AcidPublished by Elsevier ,1962
- Synthetic prefolic ABiochemical and Biophysical Research Communications, 1961
- A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counterAnalytical Biochemistry, 1960
- The Structure of “Active Formaldehyde” (N5, N10 -Methylene Tetrahydrofolic Acid)1Journal of the American Chemical Society, 1960
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTIONJournal of Biological Chemistry, 1949
- Hydrogenation of Vitamin Bc (Pteroylglutamic Acid)1 and Related PterinesJournal of the American Chemical Society, 1947
- On the mechanism of the decomposition of hydrogen peroxide by catalaseProceedings of the Royal Society of London. B. Biological Sciences, 1938