**2.12. Statistics**

726 Lipoproteins – Role in Health and Diseases

**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.

In this study, the differences were analyzed using Mann-Whitney test, Kruskal-Wallis test, paired *t* test or Wilcoxon test. A *P* value of less than 0.05 was considered significant.
