title: Immobilized purified folate-binding protein: binding characteristics and use for quantifying folate in erythrocytes.
abstract: Purified folate-binding protein from cow's milk was immobilized on monodisperse polymer particles (Dynospheres) activated by rho-toluenesulfonyl chloride. Leakage from the spheres was less than 0.1%, and the binding properties were similar to those of the soluble protein with regard to dissociation, pH optimum for binding pteroylglutamic acid, and specificity for binding various folate derivatives. We used the immobilized folate-binding protein as binding protein in an isotope-dilution assay for quantifying folate in erythrocytes. The detection limit was 50 nmol/L and the CV over a six-month period was 2.3% (means = 1.25 mumol/L, n = 15). The reference interval, for folate measured in erythrocytes of 43 blood donors, was 0.4-1.5 mumol/L.
mesh_terms: D002352:Carrier Proteins / Q000302:isolation & purification*; D004912:Erythrocytes / Q000378:metabolism*; D058973:Folate Receptors, GPI-Anchored; D005492:Folic Acid / Q000097:blood*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D011865:Radioisotope Dilution Technique; D011956:Receptors, Cell Surface / Q000302:isolation & purification*
chemical_list: D002352:Carrier Proteins; D058973:Folate Receptors, GPI-Anchored; D011956:Receptors, Cell Surface; D005492:Folic Acid