CHROMATOGRAPHIC ISOLATION AND CHARACTERIZATION OF FOLATE BINDING-PROTEINS IN PORCINE INTESTINAL EPITHELIAL BRUSH-BORDER MEMBRANE
- 1 January 1980
- journal article
- research article
- Vol. 50 (3) , 267-271
Abstract
Gel filtration studies on solubilized porcine intestinal epithelial brush border membranes labeled with [3H] folate revealed 3 distinct protein peaks, Mr [molecular size] .apprx. 25,000, Mr .apprx. 80,000 and Mr > 130,000 (listed in order of decreasing folate binding affinity). The 2 large molecular size proteins may represent polymerized forms of the Mr .apprx. 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, the cationic forms of these proteins predominant at pH 6.3. 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.This publication has 4 references indexed in Scilit:
- Aggregation of a folate-binding protein from cow's milkCarlsberg Research Communications, 1980
- High-affinity binding of folate to a protein in serum of male subjectsClinica Chimica Acta; International Journal of Clinical Chemistry, 1980
- Isolation and characterization of the folate-binding protein from cow's milkCarlsberg Research Communications, 1979
- Cooperative binding of folate to a protein isolated from cow's wheyBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978