1975 Volume 19 Issue 5 Pages 367-371
A polyacrylamide gel system for human serum lipoprotein electrophoresis was applied successfully to the separation and isolation of canine serum lipoproteins employing a preparative gel slab method combined with slicing technique.
With our gel system in which serum lipoproteins are stained prior to electrophoretic separation, the separation of lipoproteins was visible on polyacrylamide gel and the procedure was simple and accurate. Prestaining of serum lipoproteins did not disturb lipoprotein or lipoprotein lipid analyses. Canine serum lipoproteins were separated always into 4 fractions, i. e., 3 subfractions of α lipoprotein (albumin, α-1 and α-2 lipoproteins) and β lipoprotein.Alpha-1 lipoprotein is the principal fraction of serum lipoproteins of normal dogs. Lipoproteins and lipoprotein lipids were extracted from the gel blocks with sufficient recoveries to conduct further studies. Lipid extracts from each lipoprotein showed unique lipid composition differentiable from the extracts of other lipoproteins. Cross contamination of lipoprotein extracts seemed negligible if any as far as examined by lipoprotein lipid analysis or immunoelectrophoresis of the isolated lipoproteins. However, immunoelectrophoresis of whole sera and lipoprotein extracts against rabbit anti-canine immune sera showed partially discordant results suggesting complicated distribution of antigenic components.
It was concluded that with the method explored in this work further studies on canine serum lipoproteins seem to yield valuable results.
