Carrella M, Cooper A D
Proc Natl Acad Sci U S A. 1979 Jan;76(1):338-42. doi: 10.1073/pnas.76.1.338.
The binding of chylomicron remnants rat liver plasma membranes was studied. Liver membranes bound up to 8 times more remnants than they bound chylomicrons. The remnant particle appeared to bind to the membrane as a unit. Remnant binding was greatest to liver plasma membrane; only one third as much binding was observed with whole liver homogenate, and virtually no binding occurred to erythrocyte membranes or glass. Binding was saturable and had kinetics compatible with the existence of a high affinity site. Half-maximal binding occurred at 27 micron. Competitive binding studies revealed no competition with albumin, a triglyceride dispersion, cholesterol/lecithin vesicles, very low density lipoprotein, or low density lipoprotein. Some displacement of remnant binding was observed with chylomicrons and high density lipoprotein. Binding was decreased by treatment of the membranes with trypsin or the presence of heparin in the incubation medium. These studies suggest that there is a high affinity receptor for the chylomicron remnant on the surface of the hepatocyte.
对乳糜微粒残粒与大鼠肝脏质膜的结合进行了研究。肝细胞膜结合的残粒比结合的乳糜微粒多8倍。残粒颗粒似乎作为一个整体与膜结合。残粒与肝质膜的结合最强；全肝匀浆的结合量仅为其三分之一，而红细胞膜或玻璃几乎不发生结合。结合具有饱和性，其动力学与存在高亲和力位点相符。半数最大结合发生在27微米处。竞争性结合研究表明，与白蛋白、甘油三酯分散液、胆固醇/卵磷脂囊泡、极低密度脂蛋白或低密度脂蛋白不存在竞争。用乳糜微粒和高密度脂蛋白观察到残粒结合有一定程度的置换。用胰蛋白酶处理膜或在孵育培养基中加入肝素会使结合减少。这些研究表明，肝细胞表面存在乳糜微粒残粒的高亲和力受体。
