The Binding of Deoxycholic Acid to Band 3 Protein from Human Erythrocyte Membranes and to Bovine Serum Albumin
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (1) , 219-226
- https://doi.org/10.1515/bchm2.1983.364.1.219
Abstract
The binding of a H2O-soluble steroid, deoxycholic acid, to solubilized band 3 protein from erythrocyte membranes was studied by equilibrium dialysis. At acid pH, a single high affinity binding site with an association constant K = 4 .cntdot. 105 M-1 was found. The protein also showed a large number of low affinity binding sites. High affinity binding of the steroid was not observed when the pH was made alkaline or when deoxycholic acid was substituted by cholic acid. Band 3 apparently possesses a single cholesterol-binding site of high affinity and specificity. Bovine serum albumin was also found to possess a single high affinity binding site for deoxycholic acid (K = 4 .cntdot. 105 M-1). In contrast to band 3, this site is observed both at acid and alkaline pH.This publication has 3 references indexed in Scilit:
- Self-Association of Band 3-Protein from Human Erythrocyte Membranes in Aqueous SolutionsHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Interactions of Band 3-Protein from Human Erythrocyte Membranes with Cholesterol and Cholesterol AnaloguesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979