This basic science study determined the amino acid sequence of the CNBr II fragment of human ApoA-I, contributing to the structural understanding of high-density lipoproteins.
Advances ApoA-I structural mapping in HDL; leaves open any clinical translation to cardiovascular therapies.
Apolipoprotein glutamine I (apoLP-Gln-I or apoA-I) is one of the major protein constituents of human plasma high density lipoproteins. The protein has 245 amino acid residues, including 3 residues of methionine, and is lacking isoleucine, cystine, and cysteine. Cleavage of apoLP-Gln-I with cyanogen bromide yields four fragments, designated in their order of elution from Bio-Gel P-30 as CNBr I, II, III, and IV. In the present study, we report the complete amino acid sequence of the NH2-terminal fragment, CNBr II, a peptide that contains 90 amino acid residues.
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Delahunty et al. (1975) studied this question.
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