Identification of folate binding protein of mitochondria as dimethylglycine dehydrogenase. | Zendy

Arthur J. Wittwer | Zendy; Conrad Wagner | Zendy

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Identification of folate binding protein of mitochondria as dimethylglycine dehydrogenase.

Author(s) -

Arthur J. Wittwer,

Conrad Wagner

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.8.4484

Subject(s) - biochemistry , mitochondrion , chemistry , plasma protein binding , identification (biology) , biology , botany

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 1.5.99.2] 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.

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