Isolation and characterization of lipoprotein lipase activators from bovine blood serum.

Bovine serum lipoproteins were fractionated into high density and low and very low density lipoproteins by precipitation with sodium phosphotungstate and magnesium chloride. From each lipoprotein fraction seven apo C peptides were isolated by gel filtration and ion exchange chromatography. The two lipoprotein fractions probably contain identical apo C peptides but in different proportions. Two of the apo C peptides activated lipoprotein lipase from milk in vitro. Their specific activities were about 2000 times as high as that of the original serum. The apo C fraction from low-very low density lipoproteins had a specific activity three times that from high density lipoproteins. Also, the activator peptides from low and very low density lipoproteins gave one band on alkaline urea gel electrophoresis whereas corresponding peptides from high density lipoproteins were slightly heterogeneous. The low and very low density lipoproteins, therefore, seem to be the fraction of choice for isolation of activators for lipoprotein lipase.