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

1972/05/01 by H. Bryan Brewer, Samuel E. Lux, Rosemary Ronan +1 · 8 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Peroxisome Proliferator-Activated Receptors #Glycosylation and Glycoproteins Research #Protein Structure and Dynamics #Residue (chemistry) #Glutamine #Biochemistry #Peptide sequence #Amino acid #Lipoprotein #Apolipoprotein B #Chemistry #Amino acid residue #Sequence (biology) #Stereochemistry #Cholesterol #Gene

paper · pdf · doi:10.1073/pnas.69.5.1304

openalex publication_date 1972/05/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28

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.

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• Apolipoprotein A-II [wikipedia]