Z protein: isolation and characterization of multiple forms in rat liver cytosol.
Z protein: isolation and characterization of multiple forms in rat liver cytosol.
复制标题
Z 蛋白：大鼠肝细胞质中多种形式的分离和表征。
DOI：
10.1016/0003-9861(81)90300-3
复制
发表时间：
1981
影响因子：
3.9
通讯作者：
Arias,IM
中科院分区：
文献类型：
--
作者：
Trulzsch,D;Arias,IM
大鼠肝胞质溶胶的Z蛋白组分含有一种或多种与有机阴离子转运、脂肪酸代谢和氨基偶氮染料结合相关的蛋白质。为了研究这些蛋白质的可能身份并研究其功能，使用硫酸铵分级分离、凝胶过滤和制备等电聚焦纯化Z。获得了与抗Z IgG特异性反应的三种蛋白组分（pI5.2、6.0、7.3）。通过几种电泳系统测定，这三种组分是同质的。针对两种蛋白质制备的单特异性抗体与所有三种蛋白质发生特异性交叉反应。各组分与BSP的结合力不同，酸性Z与BSP的结合力最低。通过SDS-凝胶电泳测定，每个级分的分子量为12，500。三个Z蛋白条带的氨基酸分析几乎相同。异源蛋白Z可能是蛋白质与两性电解质或外源配体相互作用的结果。
The Z protein fraction of rat liver cytosol contains one or more proteins which have been associated with organic anion transport, fatty acid metabolism, and aminoazodye binding. To study the possible identity of these proteins and investigate their function, Z was purified using ammonium sulfate fractionation, gel filtration, and preparative isoelectric focusing. Three protein fractions were obtained (pI5.2, 6.0, 7.3) which reacted specifically with anti-Z IgG. These three fractions were homogenous as determined by several electrophoretic systems. Monospecific antibody prepared against two of the proteins cross-reacted specifically with all three. Each fraction bound BSP with different affinity; acidic Z bound the least BSP. The molecular weight of each fraction was 12,500 as determined by SDS-gel electrophoresis. Amino acid analyses of the three Z protein bands were virtually identical. Heterogeneity in Z probably results from interaction of the protein with ampholytes or exogenous ligands.