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The amino acid composition and sialic acid content were determined on preparations of human serum β1-lipoprotein shown to be homogeneous by analytical ultracentrifugation, electrophoresis, and gel filtration. The amino acid composition of β1-lipoprotein was compared with a number of other proteins. In contrast to structural lipoproteins, which have been reported to have an usually high content of nonpolar amino acid residues, the amino acid composition of β1-lipoprotein more closely resembles that of soluble simple proteins. A larger contribution to the lipid-binding properties of the polypeptide may be made by electrostatic interactions than by hydrophobic bonding.
Margolis et al. (Sat,) studied this question.