Purification and partial characterization of rat liver folate binding protein: cytosol I.

Cook RJ, Wagner C
Biochemistry. 1982 21 (18): 4427-34

PMID: 6897000 · DOI:10.1021/bi00261a036

The high molecular weight folate binding protein of rat liver cytosol has been purified to apparent homogeneity. Purification was achieved by using a combination of gel filtration, O-(diethylaminoethyl)cellulose chromatography, and affinity chromatography. This folate binding protein was initially identified during purification by an in vivo labeling procedure involving intraperitoneal injection of [3H]folic acid prior to sacrifice and subsequently by its ability to bind naturally reduced [3H]folate polyglutamates in vitro. A molecular weight of 210 000 was estimated by gel chromatography. This is distinct from the trifunctional formyl-methenyl-methylene synthetase of rat liver which has a molecular weight of 225 000. Sodium dodecyl sulfate electrophoresis revealed a single band with a molecular weight of about 100 000 which suggests the native protein is composed of two identical subunits. The partially purified protein contains bound tetrahydropteroylpentaglutamate.

MeSH Terms (16)

Animals Carrier Proteins Chromatography, Affinity Chromatography, DEAE-Cellulose Chromatography, Gel Chromatography, High Pressure Liquid Cytosol Folate Receptors, GPI-Anchored Formyltetrahydrofolates gamma-Glutamyl Hydrolase Glycine N-Methyltransferase Liver Molecular Weight Rats Receptors, Cell Surface Tetrahydrofolates

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