Self-association and phospholipid binding properties of iodinated apolipoprotein A-I.
Self-association and phospholipid binding properties of iodinated apolipoprotein A-I.
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碘化载脂蛋白 A-I 的自缔合和磷脂结合特性。
DOI：
10.1021/bi00365a035
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发表时间：
1986
期刊：
影响因子：
2.9
通讯作者：
Lee,AM
中科院分区：
文献类型：
--
作者：
Patterson,BW;Lee,AM
材料和方法如前所述从正常人血浆中分离载脂蛋白AI（Jonaset al.，1980），采用Sephadex G-200凝胶过滤层析，用7 M尿素平衡。在十二烷基硫酸钠存在下，纯化的蛋白质在聚丙烯酰胺凝胶电泳过程中迁移为单一条带。蛋黄磷脂酰胆碱（EYPC，V-EA型）购自Sigma Chemical Co. (St. Louis，MO），在-10 ℃下储存，不经进一步纯化使用。0.1M NaHCO 3和0.01%EDTA的标准缓冲液（pH 8.0）用于所有研究。始终使用试剂级化学品和通过Milli-Q水系统（Millipore）纯化的水。通过Lowry et al.（1951）和通过氨基酸定量（在University of Biochemistry and Molecular Biology的Ben Dunn博士的实验室中进行，
Materials and MethodsApolipoprotein AI was isolated from normal humanplasma as previously described (Jonaset al., 1980) utilizing gel fil-tration chromatography over Sephadex G-200equilibrated with 7 M urea. The purified protein migrated as a single band during polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Egg yolk phosphatidylcholine (EYPC, type V-EA) was purchased from Sigma Chemical Co.(St. Louis, MO), stored at-10 C, and used without further pu-rification. A standard buffer of 0.1 M NaHC03 and 0.01% EDTA, pH 8.0, was used for all studies. Reagent-grade chemicals and water purified by a Milli-Q water system (Millipore) were used throughout. Protein was quantitated by both the method of Lowry et al.(1951) and by amino acid quantitation (performed in the laboratory of Dr. Ben Dunn, Department of Biochemistry and Molecular Biology, Univ-