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Structural studies of rat plasma lipoproteins

, : Structural studies of rat plasma lipoproteins. Biochemistry 6(10): 3228-3241

The very low density (VLDL) and high density (HDL) lipoproteins from rat plasma were partially and totally delipidated by a n-heptane and ethanol-acetone extraction. The partially delipidated lipoproteins contained only phos-pholipid and protein. HDL, originally sedimenting as a homogeneous boundary with s20,w of 5.8 S and molecular weight 246,000, dissociated after partial extraction into 2 products with sedimentation coefficients of 5.4 and 1.9 S. These products were separated by density gradient centrifugation and only the faster contained bound phospholipids. After ethanol-acetone extraction the lipid-free protein moiety of HDL was quantitatively recovered in a soluble form that sedimented as a single boundary with S20,w of 2.1 S and had molecular weight 27,000. No changes in immunochemical properties of HDL were observed after partial or total lipid removal, although modifications were detected in optical rotatory dispersion parameters and in the response of the absorption spectra to tH changes. The properties of the major component isolated by partial or total lipid extraction from VLDL (immunoelectrophoretic behavior, sedimentation pattern, and antigenic determinants) were very similar to those observed for the phospholipid-protein residue and the lipid-free protein residue obtained from HDL. It appears that rat HDL and probably VLDL are formed by association of the small 1.9S protein with different proportions of phospholipids and neutral lipids, and that an appreciable part of the peptide chain is covered by lipids. An apparent relationship between immunochemical determinants in HDL and rat plasma albumin was found, but differences in amino acid composition and molecular size ruled out identity of these proteins.


PMID: 6056984

DOI: 10.1021/bi00862a032

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