Evidence that the low-affinity folate-binding protein in erythrocyte hemolysate is identical to hemoglobin.
Gel filtration studies on erythrocyte hemolysate demonstrated the presence of a folate binding protein, apparently of the low-affinity type, that co-elutes with hemoglobin. Further, the folate binder eluted with a low salt concentration after DEAE-Sepharose CL-6B anion-exchange chromatography of erythrocyte hemolysate at pH 6.3. The chromatographic behavior of hemoglobin labeled with [3H]folate was so similar to that of the present binder as to suggest that the folate binder in erythrocytes is in fact hemoglobin.
D002352:Carrier Proteins / Q000378:metabolism*; D002850:Chromatography, Gel; D004912:Erythrocytes / Q000378:metabolism*; D058973:Folate Receptors, GPI-Anchored; D005492:Folic Acid / Q000097:blood / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011956:Receptors, Cell Surface; D014316:Tritium
D002352:Carrier Proteins; D058973:Folate Receptors, GPI-Anchored; D006454:Hemoglobins; D011956:Receptors, Cell Surface; D014316:Tritium; D005492:Folic Acid