Sata T, Havel R J, Kotite L, Kane J P
Proc Natl Acad Sci U S A. 1976 Apr;73(4):1063-7. doi: 10.1073/pnas.73.4.1063.
A protein that binds to a lecithin-stabilized triglyceride emulsion has been separated from plasma after removal of major lipoprotein classes by ultracentrifugation at density 1.21 g/ml. This protein, rich in proline, has been purified to electrophoretic and immunochemical homogeneity by subsequent gel and ion-exchange chromatography. In native plasma and after purification, it exists as a large particle exceeding 10(6) daltons, but a single component with a molecular weight of about 74,000 is found upon polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Although the purified protein contains very little bound lipid and is not present in the major lipoprotein classes from post-absorptive individuals, it is present in chylomicrons. Its concentration in plasma varies from 12 to 41 mg/dl and is significantly correlated with that of cholesterol in lipoproteins of very low and low density but not in those of high denisty.
通过在密度为1.21 g/ml下超速离心去除主要脂蛋白类别后，从血浆中分离出一种与卵磷脂稳定的甘油三酯乳剂结合的蛋白质。这种富含脯氨酸的蛋白质通过随后的凝胶和离子交换色谱法纯化至电泳和免疫化学均一性。在天然血浆和纯化后，它以超过10(6)道尔顿的大颗粒形式存在，但在十二烷基硫酸钠聚丙烯酰胺凝胶电泳中发现一种分子量约为74,000的单一成分。尽管纯化的蛋白质含有很少的结合脂质，并且在吸收后个体的主要脂蛋白类别中不存在，但它存在于乳糜微粒中。其在血浆中的浓度在12至41 mg/dl之间变化，并且与极低密度和低密度脂蛋白中的胆固醇浓度显著相关，但与高密度脂蛋白中的胆固醇浓度无关。
