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Purification and properties of Escherichia coli dihydrofolate reductase

Biochemistry

Dec 2, 1975

D P BaccanariJ J Burchall

Abstract

Dihydrofolate reductase has been purified 40-fold to apparent homogeneity from a trimethoprim-resistant strain of Escherichia coli (RT 500) using a procedure that includes methotrexate affinity column chromatography. Determinations of the molecular weight of the enzyme based on its amin...read more

Mentioned in this Paper

Hydrogen-Ion Concentration
Macromolecular Compounds
Protein Conformation
Alloenzymes
Tetrahydrofolate Dehydrogenase
Chromatography, Affinity
Slow-K
Osmolality
Sodium Chloride, (24)NaCl
Methotrexate, (DL)-Isomer
81
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Purification and properties of Escherichia coli dihydrofolate reductase

Biochemistry

Dec 2, 1975

D P BaccanariJ J Burchall

PMID: 46

DOI: 10.1021/bi00695a006

Abstract

Dihydrofolate reductase has been purified 40-fold to apparent homogeneity from a trimethoprim-resistant strain of Escherichia coli (RT 500) using a procedure that includes methotrexate affinity column chromatography. Determinations of the molecular weight of the enzyme based on its amin...read more

Mentioned in this Paper

Hydrogen-Ion Concentration
Macromolecular Compounds
Protein Conformation
Alloenzymes
Tetrahydrofolate Dehydrogenase
Chromatography, Affinity
Slow-K
Osmolality
Sodium Chloride, (24)NaCl
Methotrexate, (DL)-Isomer
81

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