The purification and characterization of the low molecular weight human folate binding protein using affinity chromatography

S Waxman, C Schreiber


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...


Aug 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·A J Wittwer, C Wagner
May 22, 1980·Biochimica Et Biophysica Acta·J HolmJ Lyngbye
Nov 15, 1986·Archives of Biochemistry and Biophysics·H M SaidC Wagner
Aug 24, 1999·The Journal of Veterinary Medical Science·M NatsuhoriE Kokue
Oct 1, 1980·Scandinavian Journal of Clinical and Laboratory Investigation·J HolmJ Lyngbye
Feb 1, 1993·Bioscience Reports·J HolmM Høier-Madsen
Jun 1, 1977·Scandinavian Journal of Clinical and Laboratory Investigation·S I HansenJ Lyngbye

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