Abstract: A method is disclosed for detecting abnormal epitope expression of protein molecules by immunocapturing a constant number of protein molecules from a test and a reference sample using a limited amount of capturing antibodies, saturating them with its corresponding protein from the test and reference samples to provide a constant, known amount of the immobilized protein for comparison, labelling an epitope on the immobilized protein by means of a labelled probing antibody specifically reactive with the epitope and correlating any difference in labelling between the test and the reference sample to the absence or modification of the epitope in the protein of the test sample.

Abstract: Disclosed are methods that permit the determination of both lipid moiety (LM) and apolipoprotein expressed epitope immunoreactivity (EEI) of intact isolated lipoprotein species. One format of the method isolates a lipoprotein species by means of a ligand binding to a solid phase, and quantitates thereafter the LM and/or the EEI. A complementary variant format provides for nonquantitative study of a constant number of lipoprotein particles exploring the sizes of the particles (LM) and scanning the apolipoprotein epitopes (EEI). Disclosed also is a method using lipid moiety dynamics (LMD) and expressed epitopes immunoreactivity dynamics (EEID) to explore the lipid loading and unloading of the lipoprotein species during a fast-feeding cycle. Both the LMD and EEID of lipoprotein particles may be performed as a panel, individual or in any combination. This can be used to detect abnormalities in lipid metabolism that precede the hyperlipidemias associated with cardiovascular disease.