Studies on the Immunochemistry of Human Low Density Lipoproteins Utilizing an Hemagglutination Technique

Abstract

Hemagglutination is a specific and sensitive technique for investigating the purity of lipoproteins and the immunologic relationships between low density lipoprotein fractions. The Sf 10–400 and Sf 3–9 lipoprotein fractions, isolated from human serum by dextran sulfate-density gradient centrifugation procedure and repurified by centrifugation appeared to contain only lipoprotein antigens since these fractions did not stimulate the production of antibodies against other serum proteins. Cross-absorption experiments with lipoproteins carried on "tanned" cells demonstrated that the Sf 3–9 lipoprotein fraction contains all the antigenic components of the Sf 10–400 lipoprotein fraction together with additional antigenic components not found in the Sf 10–400 lipoprotein fraction. Thus Sf 3–9 and Sf 10–400 lipoprotein fractions are immunologically similar but not identical. Low density lipoproteins contain no antigens in common with the high density lipoproteins. An Sf 3–9 antiserum can be used to detect both Sf 3–9 and Sf 10–400 antigens. The Sf 3–9 lipoprotein fraction used as an antigen will detect antibodies against both Sf 3–9 and Sf 10–400 lipoprotein fractions. The Sf 3–9 and Sf 10–400 antisera did not contain immune antibodies against erythrocytes of the different blood groups or against sheep, guinea pig, dog, calf, pig, horse, and chicken erythrocytes. Normal subjects and subjects with recent myocardial infarctions had no circulating autoantibodies against the Sf 3–9 and Sf 10–400 lipoprotein fractions.

Solubilization and Properties of the Apoproteins of the Very Low- and Low-Density Lipoproteins of Human Serum*

“…The relationship between the apoproteins of VLDL and LDL has not been clearly established. Our present data (Table IV) and those of others on amino acid composition (Shore and Shore, 1962;Levy et nl., 1966;Scanu and Hughes, 1962;Levy and Frederickson, 1965; Margolis and Langdon, 1966a) and immunological behavior (Aladjem et Briner et al, 1959) tend to suggest that these apoproteins are made of closely related peptide chains. It should be noted that the difference between the amino acid analysis from different laboratories is limited to a small number of amino acids.…”