Blatter M C, James R W, Borghini I, Martin B M, Hochstrasser A C, Pometta D
Division de Diabétologie, Hôpital Cantonal Universitaire, Geneva, Switzerland.
Biochim Biophys Acta. 1990 Jan 16;1042(1):19-27. doi: 10.1016/0005-2760(90)90051-x.
This report describes the characterization of a novel rat apolipoprotein, which, as partial sequencing suggests, does not correspond to any described protein. The protein (termed PX) has an estimated molecular mass of 19.5 kDa and pI in the range 5.5-5.8. Monoclonal antibodies were obtained against protein PX and results on distribution among rat lipoproteins show it to be associated mainly with high-density lipoproteins (HDL), but also with VLDL. Immunoaffinity chromatography of total HDL shows protein PX to be included in a distinct lipoprotein particle, particularly enriched in free cholesterol, with which only traces of other apolipoproteins are associated. Immunologically crossreacting entities are found in the plasma of several species, including man. Retention of the epitope carried by the protein PX would suggest that it is of particular structural or functional importance. It remains to be established whether its function is associated with lipid metabolism.
本报告描述了一种新型大鼠载脂蛋白的特性,如部分测序所示,它与任何已描述的蛋白质都不对应。该蛋白质(称为PX)的估计分子量为19.5 kDa,pI在5.5 - 5.8范围内。获得了针对蛋白质PX的单克隆抗体,关于其在大鼠脂蛋白中的分布结果表明,它主要与高密度脂蛋白(HDL)相关,但也与极低密度脂蛋白(VLDL)相关。总HDL的免疫亲和层析显示蛋白质PX包含在一个独特的脂蛋白颗粒中,该颗粒特别富含游离胆固醇,与之相关的只有痕量的其他载脂蛋白。在包括人类在内的几种物种的血浆中发现了免疫交叉反应实体。蛋白质PX所携带表位的保留表明它具有特殊的结构或功能重要性。其功能是否与脂质代谢相关仍有待确定。