caa a22 4500 378855980 CHVBK 20180305123335.0 cr unu---uuuuu 161128e20031225xx s 000 0 eng 10.1515/BC.2003.176 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.176 The Binding of Haptoglobin to Apolipoprotein AI: Influence of Hemoglobin and Concanavalin A [Elektronische Daten] [M. S. Spagnuolo, L. Cigliano, P. Abrescia] Haptoglobin (Hp) can be purified by affinity chromatography using hemoglobin (Hb)-linked Sepharose. Elution with 8 M urea is generally performed, resulting in heavy contamination of the Hp preparation by apolipoprotein AI (ApoAI), and partial loss of Hb binding activity. Hp, separated from ApoAI, was recovered by elution with glycine-HCl at pH 3. Complexes of the isolated protein with Hb or ApoAI were detected by enzyme-linked immunosorbent assay (ELISA). Competition between the two ligands in their interaction with Hp was observed. Concanavalin A (ConA), which binds the Hp carbohydrate chains, did not influence Hp binding to ApoAI. These results suggest that changes in the plasma levels of ApoAI or Hb affect the Hp role in regulating the reverse transport of cholesterol or preventing Hb-dependent oxidative damage. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Spagnuolo M. S. aut Cigliano L. aut Abrescia P. aut Biological Chemistry Walter de Gruyter 384/12(2003-12-25), 1593-1596 1431-6730 384:12<1593 2003 384 bchm https://doi.org/10.1515/BC.2003.176 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.176 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Spagnuolo M. S. aut NATIONALLICENCE 700 1- Cigliano L. aut NATIONALLICENCE 700 1- Abrescia P. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/12(2003-12-25), 1593-1596 1431-6730 384:12<1593 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter