Abstract
To explore the potential of the common marmoset monkey (Callithrix jacchus) as a model for human plasma lipoprotein metabolism, several marmoset apolipoproteins were isolated and characterized in this study. Based on several properties, including molecular weight, amino acid composition, and sequence, the marmoset apolipoproteins are strikingly similar to human apolipoprotein (apo) A-I, A-II, C-III, and A-IV. The first 54 residues of marmoset apo A-I showed 87% sequence identity with the corresponding region of human apo A-I. Amino-terminal sequence analysis of a minor basic apo A-I isoform revealed that it contained an amino-terminal hexapeptide extension (Arg-His-Phe-Gln-Gln-) identical to that found in human proapo A-I. Like apo A-II in most nonhuman primates, marmoset apo-A-II differed from human apo A-II in that it did not contain cysteine and therefore existed as a monomer. The complete amino acid sequence of marmoset apo A-II was deduced. The protein contains 77 amino acids, as does human apo A-II, and showed an 82% identity with its human equivalent. In both species, apo C-III and E had similar amino-terminal sequences and amino acid compositions. Like human apo E, marmoset apo E contained minor sialylated isoforms. How...Continue Reading
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