Zone electrophoresis study of the bile lipoprotein complex.
Sucrose gradient column electrophoresis was performed with human hepatic and gallbladder bile. It is shown that bile phosphatidylcholines exhibit a more rapid anodic mobility than do bile salts and serum albumin. This high mobility of bile phosphatidylcholines is not due to the negatively charged lipids which are present in bile, i.e. bile salts or free fatty acids. It is demonstrated that phosphatidylcholines are associated with anionic polypeptides. Electrophoresis of reassociations between these purified polypeptides and dilaurylphosphatidylcholine showed that these anionic polypeptides are primarily responsible for the high anodic mobility of the bile lipoprotein complex. This work describes a procedure for the purification of the bile lipoprotein complex which can be useful for the study of other kinds of lipid-polypeptide associations.
D000596:Amino Acids / Q000032:analysis; D001646:Bile / Q000032:analysis*; D004586:Electrophoresis; D005230:Fatty Acids, Nonesterified; D006801:Humans; D005779:Immunodiffusion; D008074:Lipoproteins; D008823:Micelles; D010713:Phosphatidylcholines; D010743:Phospholipids
D000596:Amino Acids; D005230:Fatty Acids, Nonesterified; D008074:Lipoproteins; D008823:Micelles; D010713:Phosphatidylcholines; D010743:Phospholipids