Background: ApoB exists in human plasma in two isoforms, ApoB-48 (Chen et al., 1987) and Apo B-100 (Wei et al., 1985, Yang et al., 1986a, 1989a,b, 1990, Chen et al., 1986, Yang et al., 1990, Yang and Pownall, 1992). Apo B-100 is the major physiological ligand for the LDL receptor. Apo B-100 is a large monomeric protein, containing 4536 amino acids (m.w. 515 kDa, Yang et al., 1986b). Apo B-100 is synthesized in the liver and is required for the assembly of VLDL. It is found in LDL and VLDL after the removal of the Apo A, E and C. Apo B-48 is present in chylomicrons and their remnants. It is essential for the intestinal absorption of dietary lipids. Apo B levels correlate with the risk of coronary disease. The Apo B protein is directly involved in the retention of LDL with the arterial wall (Olofsson and Boren, 2012). Apo B-48 is synthesized in the small intestine. It comprises approximately half of the N-terminal region of ApoB-100 and is the result of posttranscriptional mRNA editing by a stop codon in the intestine not found in the liver.