title: Chromatographic isolation and characterization of folate binding proteins in porcine intestinal epithelial brush border membrane.
abstract: Gel filtration studies on solubilized porcine intestinal epithelial brush border membranes labelled with [3H] folate revealed three distinct protein peaks, Mr approximately 25 000, Mr approximately 80 000 and Mr greater than 130 000 (listed in order of decreasing folate binding affinity). The two large molecular size proteins may represent polymerized forms of the Mr approximately 25 000 peak. Folate binding proteins were eluted in front effluent after DEAE-Sepharose CL-6 B chromatography (pH 6.3, 30 mM NaCl) of a solubilized membrane preparation. This means that the cationic forms of these proteins predominate at pH 6.3. In conclusion, folate binding in brush border membranes display characteristics in many respects similar to those of high-affinity folate binding in other tissues and body fluids.
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002462:Cell Membrane / Q000032:analysis*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004848:Epithelium / Q000648:ultrastructure; D058973:Folate Receptors, GPI-Anchored; D005492:Folic Acid / Q000302:isolation & purification*; D007583:Jejunum / Q000032:analysis*; D008871:Microvilli / Q000032:analysis*; D011956:Receptors, Cell Surface; D013552:Swine
chemical_list: D002352:Carrier Proteins; D058973:Folate Receptors, GPI-Anchored; D011956:Receptors, Cell Surface; D005492:Folic Acid