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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification and characterization of tetrahydrofolate.protein complex in bovine liver.

Gel filtration of bovine liver extract on a Sephadex G-200 column resolved three macromolecular fractions with dihydropteridine reductase-dependent cytochrome c reducing activity. One of the active fractions was purified from the extract through the steps of solvent fractionation, chromatography on DEAE-Sephadex, and gel filtration. Biochemical and microbiological analyses showed that the purified complex consists of a Mr = 70,000 protein and tetrahydropteroyldiglutamate. In contrast to the extreme lability of free tetrahydropteridines the complex was quite stable against autooxidation under aerobic conditions.[1]

References

  1. Purification and characterization of tetrahydrofolate.protein complex in bovine liver. Watabe, S. J. Biol. Chem. (1978) [Pubmed]
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