PMID: 616063Jun 1, 1977Paper

Folate binding by human milk protein

Scandinavian Journal of Clinical and Laboratory Investigation
S I HansenJ Lyngbye

Abstract

Human whey was subjected to gel chromatography. Two folate binding protein fractions wer eluted: a major one (Mr congruent to 30,000) and a minor one (Mr greater than 200,000). The former folate binding fraction (FB) could be isolated from whey by means of ion exchange chromatography. Equilibrium dialysis experiments with whey and isolated FB indicated the existence of cooperatively interacting sites in folate binding. The folate analogue methotrexate inhibited folate binding. Inhibition was apparently of a competitive type since methotrexate did not reduce maximum binding capacity. Cooperativity was lost in the presence of methotrexate. Binding affinity was inversely proportional to the concentration of FB suggesting involvement of a polymerizing protein system in binding. None of the other fractions eluted on the ion exchange column could bind folate.

References

Mar 1, 1977·Clinica Chimica Acta; International Journal of Clinical Chemistry·S I HansenJ Lyngbye
Jan 1, 1975·British Journal of Haematology·S Waxman
Jan 1, 1968·Scandinavian Journal of Clinical and Laboratory Investigation·U H StenmanR Gräsbeck
Feb 1, 1970·Journal of Clinical Pathology·R E DavisA Kelly
Sep 29, 1970·Biochimica Et Biophysica Acta·J M ArmstrongW H Murphy
Sep 19, 1967·Biochimica Et Biophysica Acta·J M ArmstrongW H Sawyer

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Citations

Feb 1, 1993·Bioscience Reports·J HolmM Høier-Madsen
Oct 15, 1983·Archives of Biochemistry and Biophysics·S I HansenI Svendsen
Oct 1, 1980·Scandinavian Journal of Clinical and Laboratory Investigation·J HolmJ Lyngbye
Aug 21, 1978·Biochimica Et Biophysica Acta·S I HansenJ Lyngbye
May 1, 1979·Archives of Biochemistry and Biophysics·R Spector

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