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.
14C]Cholesterol associated with liposomes with or without anionic polypeptidic fraction was administered intravenously to the rat. The cholesterol originated from liposomes including anionic polypeptidic fraction is secreted in bile much later, is stored in liver in higher quantity, and is metabolized into bile salts in lesser quantity during the 4 hr of experimentation than the cholesterol issued from liposomes exempt of anionic polypeptidic fraction. From these results it can be postulated that the cholesterol associated with liposomes containing anionic polypeptidic fraction might be directed in a particular liver pathway. o
The anionic polypeptidic fraction is the protein constituent of the bile lipoprotein complex. Double immunodiffusion and sodium dodecyl sulfate polyacrylamide gel electrophoresis studies show that the anionic polypeptidic fraction is present in human gallstones. In terms of weight percentage, this protein accounts for 0.1% +/- 0.087 (n = 6) of the total weight of gallstones. Immunolocalization studies confirm the presence of the anionic polypeptidic fraction in human gallstones and suggest that this protein is preferentially associated with pigmented layers in gallstones. A speculative role for the anionic polypeptidic fraction in cholesterol nucleation is discussed.
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