Purification of the human anionic polypeptide fraction of the apo‐bile lipoprotein complex by zonal ultracentrifugation
- 1 December 1985
- Vol. 20 (12) , 884-889
- https://doi.org/10.1007/bf02534772
Abstract
The two main proteic constituents of the human Apo-bile lipoprotein complex (BLC), i.e., the anionic polypeptide fraction (APF) and the IgA fragments, were separated by preparative zonal ultracentrifugation using a sucrose gradient containing 1.5 mM glycodesoxycholate. The purification of the APF was verified by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis and immunology, and its amino acid composition then was determined. This procedure was used to obtain a polyclonal antiserum directed solely against the APF.This publication has 26 references indexed in Scilit:
- Solubilisation of cholesterol in human bileFEBS Letters, 1985
- Interaction of immunoglobulins and lipids in human gallblader bileBiochimie, 1981
- Effect of the polyanions precipitation on the structure of the bile lipoprotein complexBiochimie, 1980
- The apoprotein fraction of the bile lipoprotein complex: isolation, partial characterization and phospholipid binding propertiesBiochimie, 1980
- Immunological relationship between bile lipoprotein complex and high density lipoproteinBiochemical and Biophysical Research Communications, 1979
- Taurocholate- and taurochenodeoxycholate-lecithin micelles: The equilibrium of bile salt between aqueous phase and micelleBiochemical and Biophysical Research Communications, 1977
- The intermicellar bile salt concentration in equilibrium with the mixed-micelles of human bileBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1975
- Does a lecithin-polypeptide association in bile originate from membrane structural subunits?Biochimie, 1974
- Solubilisation micellaire du cholestérol par les sels biliaires et les lecithines extraits de la bile humaineBiochimie, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970