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Purification of Dihydrofolate Reductase from Human Leukocytes and from Mouse Liver and Electrofocusing on Thin-Layer Polyacrylamide Gel
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A method for the purification of dihydrofolate reductase starting upon such small
quantities as 0.05-0.3 U is described. By ammonium sulfate precipitation, gel filtration and
affinity chromatography on folate-aminohexyl-Sepharose extracts of leukocytes and mouse liver
could be purified 1,500 and 830-fold, respectively. Electrofocusing on thin-layer polyacrylamide
gels revealed two isoenzymes of mouse liver dihydrofolate reductase with pi values of 8.65 and
8.15. The purified leukocyte enzyme showed one band at pi 7.5. Addition of dihydrofolic acid or
methotrexate prior to the isoelectric focusing did not change the behavior of the enzymes. Only
addition of NADPH caused a slight decrease of the liver pi 8.15 and of the leukocyte band and the
appearance of a faint band at pi 5.4 and 5.0, respectively.
Title: Purification of Dihydrofolate Reductase from Human
Leukocytes and from Mouse Liver and Electrofocusing on
Thin-Layer Polyacrylamide Gel
Description:
A method for the purification of dihydrofolate reductase starting upon such small
quantities as 0.
05-0.
3 U is described.
By ammonium sulfate precipitation, gel filtration and
affinity chromatography on folate-aminohexyl-Sepharose extracts of leukocytes and mouse liver
could be purified 1,500 and 830-fold, respectively.
Electrofocusing on thin-layer polyacrylamide
gels revealed two isoenzymes of mouse liver dihydrofolate reductase with pi values of 8.
65 and
8.
15.
The purified leukocyte enzyme showed one band at pi 7.
5.
Addition of dihydrofolic acid or
methotrexate prior to the isoelectric focusing did not change the behavior of the enzymes.
Only
addition of NADPH caused a slight decrease of the liver pi 8.
15 and of the leukocyte band and the
appearance of a faint band at pi 5.
4 and 5.
0, respectively.
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