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Studies on Human Serum ß₁-Lipoprotein

I. AMINO ACID COMPOSITION

From the ¹ From the Department of Physiological Chemistry, The Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205

The amino acid composition and sialic acid content were determined on preparations of human serum ß₁-lipoprotein shown to be homogeneous by analytical ultracentrifugation, electrophoresis, and gel filtration. The amino acid composition of ß₁-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 ß₁-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.

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