Ponsin G, Gotto A M, Utermann G, Pownall H J
Biochem Biophys Res Commun. 1985 Dec 31;133(3):856-62. doi: 10.1016/0006-291x(85)91213-6.
Several isoforms of apoprotein A-I [apoA-I], the major apoprotein of high density lipoproteins [HDL], have been described. We compared the in vivo and in vitro properties of normal human apoA-I with those of apoA-I [Lys107----0]. Fluorescence and circular dichroic spectra showed that deletion of Lys107 decreases apoprotein self-association. In vivo metabolic studies in the rat indicated that the interaction of apoA-I [Lys107----0] with HDL was lower than normal. We conclude that deletion of Lys107 results in a reorganization of the apoprotein structure that decreases its potential to form hydrophobic associations.
已描述了高密度脂蛋白（HDL）的主要载脂蛋白载脂蛋白A-I [apoA-I]的几种同工型。我们比较了正常人apoA-I与apoA-I [Lys107----0]的体内和体外特性。荧光和圆二色光谱表明，Lys107的缺失会降低载脂蛋白的自我缔合。在大鼠体内进行的代谢研究表明，apoA-I [Lys107----0]与HDL的相互作用低于正常水平。我们得出结论，Lys107的缺失导致载脂蛋白结构的重组，从而降低了其形成疏水缔合的潜力。
