Identification of folate binding protein of mitochondria as dimethylglycine dehydrogenase.

Wittwer AJ, Wagner C
Proc Natl Acad Sci U S A. 1980 77 (8): 4484-8

PMID: 6159630 · PMCID: PMC349868 · DOI:10.1073/pnas.77.8.4484

The folate-binding protein of rat liver mitochondria [Zamierowski, M. & Wagner, C. (1977) J. Biol. Chem. 252, 933-938] has been purified to homogeneity by a combination of gel filtration, DEAE-cellulose, and affinity chromatography. This protein was assayed by its ability to bind tetrahydro[3H]folic acid in vitro. the purified protein contains tightly bound flavin and has a molecular weight of about 90,000 as determined by sodium dodecyl sulfate electrophoresis. This protein also displays dimethylglycine dehydrogenase [N,N-dimethylglycine: (acceptor) oxidoreductase (demethylating), EC] activity which copurifies with the folate-binding activity. It is suggested that the role of the tetrahydrofolic acid is to accept the formaldehyde produced during the course of the reaction.

MeSH Terms (11)

Animals Carrier Proteins Dimethylglycine Dehydrogenase Flavoproteins Folic Acid Mitochondria, Liver Mitochondrial Proteins Oxidoreductases, N-Demethylating Rats Sarcosine Spectrum Analysis

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