The purification and characterization of the low molecular weight human folate binding protein using affinity chromatography.
The low molecular weight folate binding protein (FABP) has been purified 1000-fold to a specific activity of 7.2 gamma g of pteroylglutamic acid (PGA) bound per mg of protein. This purified FABP represents two protein bands that bind PGA on polyacrylamide disc gel electrophoreis, elutes from DEAE-cellulose in 0.001 M phosphate buffer, stains positive with PAS, Elutes from concanavalin A Sepharose affinity columns with methyl alpha-mannoside, and shows three major peaks (pl =6.8, 7.5, 8.2) by isotric focusing. The binding of PGA to purified FABP dependent on pH and is inhibited by urea...
D002352:Carrier Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002986:Clinical Trials as Topic; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005492:Folic Acid / Q000378:metabolism; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008895:Milk, Human; D008970:Molecular Weight; D014508:Urea / Q000494:pharmacology
D002352:Carrier Proteins; D014508:Urea; D005492:Folic Acid