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. 1972 May;69(5):1304–1308. doi: 10.1073/pnas.69.5.1304

Amino Acid Sequence of Human apoLp-Gln-II (apoA-II), an Apolipoprotein Isolated from the High-Density Lipoprotein Complex

H B Brewer Jr 1, S E Lux 1, R Ronan 1, K M John 1
PMCID: PMC426687  PMID: 4338591

Abstract

An apolipoprotein, designated by its carboxyl-terminal residue as apoLp-Gln-II, has been isolated from the human high-density lipoprotein family, and its complete aminoacid sequence was determined. The apoprotein, one of the two major apoproteins of this family, is composed of two identical polypeptide chains, each containing 77 amino acids. The two polypeptide chains are connected by a single disulfide bridge at position 6 in the sequence. The minimum molecular weight of the intact apoprotein is 17,380. The amino-terminal residue of each chain is pyrrolidone carboxylic acid, and the carboxyl-terminal residue is glutamine.

Keywords: pyrrolidone carboxylic acid, lipid-protein interactions, human blood plasma, automated Edman degradations, protein structure

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Selected References

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