The purification of rat and sheep liver dihydropteridine reductases by affinity chromatography on methotrexate-sepharose. 1978

S Webber, and T L Deits, and W R Snyder, and J M Whiteley

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008727 Methotrexate An antineoplastic antimetabolite with immunosuppressant properties. It is an inhibitor of TETRAHYDROFOLATE DEHYDROGENASE and prevents the formation of tetrahydrofolate, necessary for synthesis of thymidylate, an essential component of DNA. Amethopterin,Methotrexate Hydrate,Methotrexate Sodium,Methotrexate, (D)-Isomer,Methotrexate, (DL)-Isomer,Methotrexate, Dicesium Salt,Methotrexate, Disodium Salt,Methotrexate, Sodium Salt,Mexate,Dicesium Salt Methotrexate,Hydrate, Methotrexate,Sodium, Methotrexate
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009247 NADH, NADPH Oxidoreductases A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6. Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D004093 Dihydropteridine Reductase An enzyme that catalyzes the reduction of 6,7-dihydropteridine to 5,6,7,8-tetrahydropteridine in the presence of NADP+. Defects in the enzyme are a cause of PHENYLKETONURIA II. Formerly listed as EC 1.6.99.7. 6,7-Dihydropteridine Reductase,6,7 Dihydropteridine Reductase,Reductase, 6,7-Dihydropteridine,Reductase, Dihydropteridine
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012685 Sepharose Agarose,Sepharose 4B,Sepharose C1 4B,4B, Sepharose C1,C1 4B, Sepharose

Related Publications

S Webber, and T L Deits, and W R Snyder, and J M Whiteley
May 1977, Analytical biochemistry,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
August 1996, Archives of biochemistry and biophysics,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
August 1978, Biochimica et biophysica acta,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
July 1989, Journal of chromatography,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
November 1996, Journal of neuroscience methods,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
August 1980, Journal of chromatography,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
May 1970, FEBS letters,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
February 1977, FEBS letters,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
March 1985, Journal of lipid research,
S Webber, and T L Deits, and W R Snyder, and J M Whiteley
October 1979, Biochemical and biophysical research communications,
Copied contents to your clipboard!