**2.11. Assay of concentrations of Apo CIII, apolipoprotein AI (Apo AI) and apolipoprotein B100**

Concentrations of Apo CIII, Apo AI and Apo B100 in the platelet lysate were assayed by ELISA using commercially available assay kits for Apo CIII (AssayPro, St. Charles, MO), Apo AI (Mabtech AB, Nacka Strand, Sweden) and Apo B100 (Mabtech AB), respectively.

**Figure 1.** Characterization of the LMW activator produced from Apo CIII. **A.** MAPP formation using Apo CIII. To prepare LMW activator, 10 g/ml Apo CIII was treated with 0.1 unit/ml thrombin or 1 unit/ml trypsin, and then diluted serially x10. The activity of each diluted sample as LMW activator was examined. **B.** MONO S cation exchange chromatography of thrombin-treated Apo CIII (10 g). MAPPs were generated using each fraction at a dilution of x102 and one of the precursors of MAPPs. **C.** MONO S cation exchange chromatography of trypsin-treated apolipoprotein CIII (10 g/ml). MAPPs were generated using each fraction at a dilution of x104 and one of the precursor of MAPPs. **D.** Superdex peptide gel filtration of thrombin-treated Apo CIII (10g/ml). Formation of MAPPs was achieved using each fraction at a dilution of x102 and one of the precursors of MAPPs. **E.** Superdex peptide gel filtration of trypsin-treated Apo C-III (10 g/ml). Formation of MAPPs was achieved using each fraction at a dilution of x104 and one of the precursors of MAPPs. **F.** Molecular weight determination of the LMW activator with comparisons with those of Apo CIII-derived peptides. **G.** Amino acid sequence of Apo CIII, distributions of basic (+) and acidic (-) amino acids and sugar binding amino acid (T74) in Apo CIII. The amino acid sequence is cited from the database of GenPex (NCBI Protein DataBase, http://www.ncbi.nlm.nih.gov/protein). **A**, **B**, **C**, **D** and **E** were performed using the precursor of s-MAPP.
