Ligand binding and polymerization characteristics of human milk folate binding protein depend on concentration of purified protein and presence of amphiphatic substances

Two folate binding proteins are present in human milk; one of 27 kDa is a cleavage product of the other one (100 kDa) which possesses a hydrophobic membrane anchor. A drastic change of radioligand binding characteristics and appearance of aggregated weak-radioligand affinity forms on gel filtration...

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Veröffentlicht in:	Bioscience reports 2003-04, Vol.23 (2-3), p.77-85
Hauptverfasser:	Holm, Jan, Hansen, Steen Ingemann
Format:	Artikel
Sprache:	eng
Schlagworte:	Carrier Proteins - chemistry Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cetrimonium Cetrimonium Compounds - chemistry Chromatography, Gel Dialysis Female Folate Receptors, GPI-Anchored Folic Acid - chemistry Folic Acid - metabolism Humans Ligands Milk Proteins - chemistry Milk Proteins - isolation & purification Milk Proteins - metabolism Milk, Human - chemistry Octoxynol - chemistry Phosphatidylcholines - chemistry Polymers Protein Binding Radioligand Assay Receptors, Cell Surface
Online-Zugang:	Volltext
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