Heinderyckx M, Jacobs P, Bollen A
Service de Génétique Appliquée, University of Brussels, Belgium.
Mol Biol Rep. 1988;13(4):225-32. doi: 10.1007/BF00788175.
Human haptoglobin (Hp alpha 2 beta) was synthesized in insect cells using the baculovirus Autographa californica nuclear polyhedrosis virus (AcNPV) as an expression vector. Viruses carrying the proHp alpha 2 beta cDNA, either fused or non fused to viral polyhedrin DNA sequences, expressed intracellularly low levels of unglycosylated and non maturated haptoglobin. On the contrary, recombinant viruses containing the preproHp alpha 2 beta cDNA directed the expression of high levels of prohaptoglobin. To a large extent, the uncleaved product was found in the culture medium as a glycosylated molecule. Despite the lack of maturation into subunits, the secreted recombinant prohaptoglobin was able to bind hemoglobin in vitro, although less efficiently than plasma-derived haptoglobin.
利用杆状病毒苜蓿银纹夜蛾核型多角体病毒（AcNPV）作为表达载体，在昆虫细胞中合成了人触珠蛋白（Hpα2β）。携带前Hpα2β cDNA的病毒，无论是否与病毒多角体蛋白DNA序列融合，在细胞内表达的未糖基化且未成熟的触珠蛋白水平都很低。相反，含有前原Hpα2β cDNA的重组病毒能指导高水平的前触珠蛋白表达。在很大程度上，未切割的产物以糖基化分子的形式存在于培养基中。尽管未成熟为亚基，但分泌的重组前触珠蛋白在体外能够结合血红蛋白，不过其效率低于血浆来源的触珠蛋白。
