Effect of glycation of low-density lipoprotein on the immunological determination of apolipoprotein B.
Non-enzymatic glycation of low-density lipoprotein (LDL) may contribute to the premature atherogenesis of patients with diabetes mellitus. To assess whether glycation of apolipoprotein B, the predominant protein of LDL, interferes with the ability to immunologically quantify this protein, we prepared and purified glycated LDL by incubating normal plasma samples with high concentrations of glucose. Although both the plasma and the LDL specimens incubated with glucose contained significantly more glycated protein than control specimens, the quantitative interaction of an apolipoprotein B-specific antibody with glycated vs nonglycated LDL was not significantly different. We conclude that apolipoprotein B can be accurately quantified immunologically despite the presence of clinically excessive degrees of LDL glycation.
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Department of Pathology, Hospital of the University of Pennsylvania, Philadelphia 19104.
Wilding
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D001055:Apolipoproteins B / Q000097:blood*; D019270:Fructosamine; D017127:Glycation End Products, Advanced; D006595:Hexosamines / Q000097:blood; D006801:Humans; D007118:Immunoassay; D008077:Lipoproteins, LDL / Q000097:blood*; D000093844:Glycated Proteins
D001055:Apolipoproteins B; D019270:Fructosamine; D017127:Glycation End Products, Advanced; D006595:Hexosamines; D008077:Lipoproteins, LDL; C031797:glycated lipoproteins, LDL; D000093844:Glycated Proteins