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By Rodolfo Paoletti; David Kritchevsky

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1982). The apoE allele frequencies have also been assessed in different populations (Assmann et al, 1984; Bouthillier etal, 1983; Breslow and Zannis, 1987; Cumming and Robertson, 1984; Ehnholm etal, 1986; Eto etal, 1986a; Ordovas etal, 1987; Utermann etal, 1982; Wardell etal, 1982) around the world. 077. apoE phenotype frequencies were: E4/4, 3; E3/3, 60; E2/2, 6; E4/3, 23; E4/2, 2; and E3/2, 12 (Utermann et al, 1982). 12 (Wardell etal, 1982). 117, respectively, from 576 Japanese subjects from Asahikawa (Eto etal, 1896a) were significantly different from those of the other populations studied.

A receptor binding domain in this region was also predicted by hydrophobicity and hydrophobic moment calculations (DeLoof etal, 1986). As already mentioned, the sequence of apoE between residues 142-149 has 63% homology with the region between residues 3359 and 3366 of apoB-100 (Fig. 3C). , 1986), as well as by ligand blotting using synthetic apoE peptides (Cardin et al, 1986). Both methods identified heparin binding sites between residues 142 and 147 located within the receptor binding domain of apoE (DeLoof et al, 1986; Innerarity etal, 1983; Weisgraber etal, 1983).

Proc. Natl. Acad. Sci. SA. 81, 4539-4543. Das, H. , Bruns, G. A. , Karathanasis, S. , and Breslow, J. L. (1985). J. Biol. Chem. 260, 6240-6246. , and Ontko, J. A. (1980). Biochim. Biophys. Acta 638, 347-359.

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