Journal of Lipid Research, Vol. 7, 295-306, March 1966
Copyright © 1966 by Lipid Research, Inc.

Forms of human serum high density lipoprotein protein

A. Scanu

Department of Medicine, The University of Chicago School of Medicine, Chicago, Illinois

Delipidation by ethanol-diethyl ether at -10°C of human serum high-density lipoprotein (HDL, d 1.063-1.21) or of its subclasses HDL₂ (d 1.063-1.120) and HDL₃ (d 1.120-1.21), yielded proteins—P, P₂, and P₃—containing 3% phospholipid (largely lecithin) and 3.3% carbohydrate (glucosamine:l-focuse:d-galactose, d-mannose:sialic acid, 1.00:41 : 0.56:0.31).

Solubility data and analytical ultracentrifugal analyses indicated that, upon lipid removal, HDL protein aggregates readily; the aggregation is dependent upon pH and ionic strength of the solvent medium. Subunits of 21,000 mol wt were obtained by acetylation or addition of sodium dodecyl sulfate (SDS).

HDL and P elicited in the rabbit a similar immunological response. By agar gel immunoelectrophoresis both anti-HDL and anti-P sera detected a major and two minor antigenic determinants in HDL, HDL₃, P, P₂, and P₃. HDL₂, antigenically homogeneous, gave an immunoelectrophoretic pattern of HDL₃ upon mixing with P. P, P₂, and P₃ exhibited a single antigenic determinant after treatment with SDS (0.5 m) or upon acetylation.

Native or delipidated forms of HDL, HDL₂, and HDL₃ were separated by vertical starch gel electrophoresis into several components, which showed identical reactions against anti-HDL or anti-P sera.

The data suggest that (a) the proteins of HDL, HDL₂, and HDL₃ are made of subunits, probably identical, of an average molecular weight of 21,000; (b) the difference in antigenic behavior between HDL₂ and HDL₃ is due to the presence in the latter of a lipid-poor protein; (c) antigenic polymorphism of P is probably related to the presence in solution of monomeric and polymeric forms having different reactivity against anti-HDL and anti-P sera.

Supplementary key words serum • high density lipoprotein • delipidation • carbohydrate content • solubility • amino acid analysis • ultracentrifugal properties • immunoelectrophoresis • starch gel immunoelectrophoresis • protein subunits

Submitted on June 2, 1965
Accepted on October 27, 1965

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