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JBC, Vol. 250, Issue 1, 182-190, Jan, 1975
R. S. Shulman, P. N. Herbert, K. Wehrly and D. S. Fredrickson
C-I was prepared from very low density lipoproteins of patients with
familial type V hyperliporproteinemia. Peptides from tryptic digests of
unmodified and succinylated C-I, chymotryptic peptides, and the products of
cayanogen bromide cleavage were isolated and characterized. Sequence
analysis of tryptic peptides was performed by the dansyl
(5-dimethylaminonaphthalene-1-sulfonyl) technique and hydrolytic
regeneration of the amino acid residues from the phenylthiocarbamyl
derivatives. Alignment of the tryptic fragments within the cyanogen bromide
and succinyl-tryptic peptides was confirmed by the overlap chymotryptic
peptides. The complete amino acid sequence of C-I, 57 residues in length,
does not reveal any obvious basis for its lipophilic properties.
Thf complete amino acid sequence of C-I (apoLp-Ser), an apolipoprotein from human very low density lipoproteins
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