Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence

Porcine liver dihydrofolate reductase has been purified 18,000-fold to homogeneity. The properties of the purified enzyme were compared to those of dihydrofolate reductase from L1210 cells, the only mammalian reductase for which complete amino acid sequence data are available. The enzymes are very s...

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Bibliographic Details
Published in:The Journal of biological chemistry 1979-11, Vol.254 (22), p.11475-11484
Main Authors: Smith, S L, Patrick, P, Stone, D, Phillips, A W, Burchall, J J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Animals
Cattle
Chickens
Kinetics
Leukemia L1210 - enzymology
Liver - enzymology
Mice
Molecular Weight
Species Specificity
Substrate Specificity
Swine
Tetrahydrofolate Dehydrogenase - isolation & purification
Tetrahydrofolate Dehydrogenase - metabolism
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Summary:Porcine liver dihydrofolate reductase has been purified 18,000-fold to homogeneity. The properties of the purified enzyme were compared to those of dihydrofolate reductase from L1210 cells, the only mammalian reductase for which complete amino acid sequence data are available. The enzymes are very similar when compared on the basis of mechanism and kinetic constants, molecular weights, isoelectric points, and stimulation by salt. A comparison of the amino acid sequences of both enzymes shows an overall identity of 89%. Thus, the similarities seen in inhibitor-binding profiles of mammalian enzymes reflect the close relationship of these enzymes at the molecular level.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)86510-9