Apoc-III-beta-galactosidase hybrid distinguishes between VLDL and LDL phospholipids.
Apoc-III-beta-galactosidase hybrid distinguishes between VLDL and LDL phospholipids.
复制标题
Apoc-III-β-半乳糖苷酶杂合体可区分 VLDL 和 LDL 磷脂。
DOI：
10.1006/bbrc.1995.1877
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
McConathy,WJ
中科院分区：
文献类型：
--
作者：
Trieu,VN;McConathy,WJ
构建了指导前载脂蛋白C-Ⅲ与β-半乳糖苷酶融合表达的质粒。携带该构建体的大肠杆菌产生具有完全β-半乳糖苷酶活性的杂合体，占总细胞蛋白的0.6%。纯化的preapoC-III-β-半乳糖苷酶杂合物与极低密度脂蛋白特异性结合，并被纯化的apoC-III抑制。未观察到与低密度脂蛋白的结合。结合是由极低密度脂蛋白的磷脂介导的，因为杂交体对磷脂具有特异性亲和力，对甘油三酯、胆固醇酯或胆固醇没有可检测的亲和力。差异结合表明极低密度脂蛋白的磷脂和低密度脂蛋白的磷脂之间存在差异。
A plasmid directing the expression of preapolipoprotein C-III fused to β-galactosidase was constructed. Escherichia coli harboring this construct produced the hybrid, with full β-galactosidase activity, at 0.6% of total cellular protein. Purified preapoC-III-β-galactosidase hybrid exhibited specific binding to very low density lipoproteins, which was inhibited by purified apoC-III. No binding to low density lipoproteins was observed. Binding was mediated by the phospholipids of very low density lipoproteins, as the hybrid had a specific affinity for phospholipids and no detectable affinity for triglycerides, cholesteryl esters, or cholesterol. The differential binding suggests that there are differences between the phospholipids of very low density lipoproteins and the phospholipids of low density lipoproteins.