Lorenzetti R, Sidoli A, Palomba R, Monaco L, Martineau D, Lappi D A, Soria M
FEBS Lett. 1986 Jan 6;194(2):343-6. doi: 10.1016/0014-5793(86)80114-4.
The human apoAI gene was expressed in E. coli by in-frame fusion to a modified beta-galactosidase gene present in plasmid pUR291. The fused beta-galactosidase-apoAI gene product was expressed at a high level and was recognized by an anti-human apoAI antiserum. Besides the fused protein, at least one degradation product having an Mr similar to that of beta-galactosidase was present in high amounts in bacterial extracts. These results and those of a pulse-chase experiment indicate that degradation took place only in the apoAI moiety of the chimeric protein.
通过与质粒pUR291中存在的修饰β-半乳糖苷酶基因进行读码框融合,人载脂蛋白AI(apoAI)基因在大肠杆菌中得以表达。融合的β-半乳糖苷酶-apoAI基因产物高水平表达,并能被抗人apoAI抗血清识别。除融合蛋白外,细菌提取物中还大量存在至少一种分子量与β-半乳糖苷酶相似的降解产物。这些结果以及脉冲追踪实验的结果表明,降解仅发生在嵌合蛋白的apoAI部分。