Paolucci M, Callard I P
Department of Biology, Boston University, MA 02215, USA.
Comp Biochem Physiol B Biochem Mol Biol. 1995 Mar;110(3):583-8. doi: 10.1016/0305-0491(94)00177-v.
Very low density lipoproteins (VLDL) (d < 1.006), low density lipoproteins (LDL) (1.006 < d < 1.063), and high density lipoproteins (HDL) (1.063 < d < 1.21) were isolated by ultracentrifugation from the plasma of female and male Chrysemys picta. The protein components of lipoproteins (apolipoproteins) were analysed by electrophoresis in denaturing polyacrylamide gradient gel. Gel filtration chromatography, electroelution from gradient gel and two dimensional electrophoresis were utilized to partially purify and characterized the main apolipoproteins. A 350 kDa Apo B-like protein was found associated with VLDL and LDL fractions. In HDL, Apo AI was the main protein component which, after purification on Sephadex G-200, showed the same electrophoretic mobility as human Apo AI (28 kDa). When analysed by two dimensional electrophoresis, Apo AI gave a pI value of 5.2. A 36 kDa apolipoprotein was purified from VLDL fraction. The purified putative Apo E showed an electrophoretic mobility slightly lower than human Apo E (34 kDa). The only sex difference observed was a band in the female bottom fraction (d > 1.21) with similar electrophoretic mobility to vitellogenin.
通过超速离心从雌性和雄性锦龟的血浆中分离出极低密度脂蛋白（VLDL）（d < 1.006）、低密度脂蛋白（LDL）（1.006 < d < 1.063）和高密度脂蛋白（HDL）（1.063 < d < 1.21）。通过在变性聚丙烯酰胺梯度凝胶中进行电泳分析脂蛋白的蛋白质成分（载脂蛋白）。利用凝胶过滤色谱、从梯度凝胶中电洗脱和二维电泳对主要载脂蛋白进行部分纯化和表征。发现一种350 kDa的载脂蛋白B样蛋白与VLDL和LDL组分相关。在HDL中，载脂蛋白AI是主要的蛋白质成分，在Sephadex G - 200上纯化后，其电泳迁移率与人类载脂蛋白AI（28 kDa）相同。通过二维电泳分析时，载脂蛋白AI的pI值为5.2。从VLDL组分中纯化出一种36 kDa的载脂蛋白。纯化后的假定载脂蛋白E的电泳迁移率略低于人类载脂蛋白E（34 kDa）。观察到的唯一性别差异是在雌性底部组分（d > 1.21）中有一条带，其电泳迁移率与卵黄蛋白原相似。
