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

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 v.eight of the intact apoprotein is 17,380. The amino-terminal residue of each chain is pyrrolidone carboxylic acid, and the carboxylterminal residue is glutamine.

13 C Nuclear Magnetic Resonance Spectroscopy of Native and Recombined Lipoproteins

“…It has been previously pointed out that apoC-III and apoA-II contain several pairs of sequentially adjacent amino acids whose side chains are oppositely charged (38). The ionic interaction of these oppositely charged side chains with the zwitterionic polar head group has been suggested as a mechanism of protein-lipid binding (51).…”

Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates

“…Human apoAII consists of 2 identical chains linked together by a disulfide bridge. 57 After secretion, apoAII is mainly incorporated into high-density lipoprotein particles containing a variable amount of apoAI and apoAII. 58 The functional role of apoAII in vivo is still unclear, although in vitro and in vivo studies have suggested its proatherogenic effect.…”

In vitro activation of the enzymic activity of hepatic lipase by apoA‐II

“…ApoA-II and apoC-II were purified as in [17,18]. ApoA-II was dissolved in 6 M guanidine, 0.01 M Tris, 0.1 M NaCI (pH 7.4) and dialyzed against 0.01 M ammonium bicarbonate (pH 8.6).…”