A combination of cation exchange and ligand-affinity chromatography for purification of two molecular species of the folate binding protein in human milk, one equipped with a hydrophobic glycosyl phosphatidylinositol tail: Characterization of hydrophobicity and electrical charge

Bioscience Reports

Volumn 22, Issue 3-4, 2002, Pages 443-454

  Holm, Jan ^a,d   Hansen, Steen Ingemann ^b   Høier Madsen, Mimi ^c  

^a HERNING HOSPITAL   (Denmark)

^b HILLERØD HOSPITAL   (Denmark)

^c STATENS SERUM INSTITUT   (Denmark)

^d Bornholm Hospital   (Denmark)

Author keywords

Chromatographic separation of two molecular forms of protein; Human milk folate binding proteins; Hydrophobicity and multiple isoelectrical points at pH 7 9

Indexed keywords

FOLATE BINDING PROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL; TRITON X 100;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CHROMATOFOCUSING; ELECTRICITY; ELUTION; GEL FILTRATION; HUMAN; HYDROPHOBICITY; ION EXCHANGE CHROMATOGRAPHY; ISOELECTRIC POINT; MILK; MOLECULAR SIZE; NONHUMAN; PH; PROTEIN DEGRADATION; PROTEIN PURIFICATION;

CARRIER PROTEINS; CATIONS; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, ION EXCHANGE; ELECTROCHEMISTRY; FEMALE; GLYCOSYLPHOSPHATIDYLINOSITOLS; HUMANS; HYDROPHOBICITY; LIGANDS; MILK, HUMAN; RECEPTORS, CELL SURFACE;

EID: 0036626248     PISSN: 01448463     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020922226362     Document Type: Article

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