Abstract
Publisher Summary The structure of plasma lipoproteins has revealed the presence of a protein of very high molecular weight in VLDL and LDL, which was termed apolipoprotein B. This chapter describes the techniques for purifying and characterizing the B-48 apolipoprotein. The B apolipoproteins share certain biochemical properties, such as those of intrinsic membrane proteins. ApoB-48 is purified from the triglyceride-rich lipoproteins of intestinal origin, the chylomicrons. The amino acid analysis reveals the Schlieren peak that coincides with cysteic acid, which is believed to be due to the passage of two solvent fronts through the flow cell. The results indicate that weight estimates for B-48 are strongly influenced by two factors during electrophoresis: protein load and gel concentration. Based on this analysis, a set of conditions for estimating the molecular weights of B proteins has been established, using SDS-PAGE that forms the basis for the centile system of nomenclature.
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