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. 1974 Sep;71(9):3631–3634. doi: 10.1073/pnas.71.9.3631

The Primary Structure of High Density Apolipoprotein-Glutamine-I

H Nordean Baker 1,2, Thomas Delahunty 1,2, Antonio M Gotto Jr 1,2, Richard L Jackson 1,2
PMCID: PMC433829  PMID: 4372630

Abstract

The major protein constituent of human plasma high density lipoproteins has been isolated and its complete amino-acid sequence determined. The protein, designated apolipoprotein-glutamine-I by the presence of carboxyl-terminal glutamine, is a single polypeptide chain of 245 amino-acid residues, including three residues of methionine. The protein is devoid of cysteine, cystine, and isoleucine. Cleavage of apolipoprotein-glutamine-I with cyanogen bromide yields four fragments with 94, 90, 36, and 25 amino acids. The amino-acid sequence of each fragment was determined by conventional methods, with proteolytic digestion with trypsin, chymotrypsin, and thermolysin. The alignment of the cyanogen bromide fragments was determined by the isolation of the methionine-containing tryptic peptides from apolipoprotein-glutamine-I.

Inspection of the sequence of apolipoprotein-glutamine-I suggests an interesting distribution of amino acids that may account for its helical structure and its ability to bind and transport lipid.

Keywords: primary amino-acid sequence, lipid-protein interaction, α-helical structure

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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