Immunological Properties of Bovine Serum Lipoproteins and Chemical Analysis of Their Protein Moieties

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Abstract
Four classes of bovine serum lipoproteins were isolated by precipitation with dextran sulfate, ultracentrifugation, and preparative electrophoresis on polyacrylamide gel. Very low density lipoprotein (d less than 1.019 g/ml) was related immunologically to low density lipoprotein-two (d 1.039 to 1.060 g/ml) and high density lipoprotein (d 1.060 to 1.210 g/ml) was related immunologically to low density lipoprotein-one (d 1.019 to 1.039 g/ml), but the two pairs were immunologically distinct. The major N-terminal amino acid of both high density lipoprotein and low density lipoprotein-one was aspartic acid, and that of low density lipoprotein-two was glutamic acid. Very low density lipoprotein had both aspartic acid and glutamic acid as the major N-terminal amino acids. None of the lipoproteins was identical with any other with respect to amino acid composition, but high density lipoprotein and low density lipoprotein-one were similar to each other and different from low density lipoprotein-two. Very low density lipoprotein was similar to both low density lipoprotein-one and low density lipoprotein-two. It is concluded that the proteins of high density lipoprotein and of low density lipoprotein-one are related and are different from that of low density lipoprotein-two. The protein of very low density lipoprotein is related to that of low density lipoprotein-two but may contain polypeptides of high density lipoprotein or low density lipoprotein-one.

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