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Abstract
This chapter describes in detail the methods used for the isolation of the polipoprotein C (apoC) proteins in a homogeneous state. These methods include preparative isoelectric focusing (IEF), high-performance liquid chromatography (HPLC), and chromatofocusing. Human apoC-I contains 57 amino acid residues whose sequence is determined from the protein, and the apolipoprotein lacks cysteine, histidine, and tyrosine. Human apoC-II, the activator protein for lipoprotein lipase, contains 79 amino acid residues. The amino acid sequence of this protein has been determined from the protein 17 and DNA, and the protein lacks cysteine and histidine. Human apoC-III is a 79 amino acid glycoprotein of known primary structure; however, the amino acid sequence as determined from the DNA is slightly different than that reported earlier from the protein sequence. The protein has an amino acid molecular weight of 8746 and lacks cysteine and isoleucine. The carbohydrate attachment is 1 residue each of galactose and galactosamine and either 0 (apoCIII-0), 1 (apoC-III-1), or 2 (apoC-III-2) residues of sialic acid.
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