Ward P P, May G S, Headon D R, Conneely O M
Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.
Gene. 1992 Dec 1;122(1):219-23. doi: 10.1016/0378-1119(92)90054-s.
The production and secretion of human lactoferrin (hLF) in Aspergillus nidulans is described. The hLF cDNA was expressed under the control of the strong ethanol-inducible alcohol dehydrogenase (alcA) promoter. Recombinant hLF (re-hLF) is produced at levels up to 5 micrograms/ml. Approximately 30% of the re-hLF produced in this system is secreted into the growth medium. The re-hLF is indistinguishable from native hLF with respect to size and immunoreactivity. Furthermore, re-hLF is functional by the criterion of iron-binding capacity. The A. nidulans expression system offers an inexpensive, convenient method for the controlled production of mg amounts of biologically active mammalian glycoproteins.
本文描述了构巢曲霉中人类乳铁蛋白（hLF）的生产和分泌情况。hLF cDNA在强乙醇诱导型乙醇脱氢酶（alcA）启动子的控制下表达。重组hLF（re-hLF）的产量高达5微克/毫升。该系统中产生的re-hLF约有30%分泌到生长培养基中。re-hLF在大小和免疫反应性方面与天然hLF没有区别。此外，根据铁结合能力的标准，re-hLF具有功能。构巢曲霉表达系统为可控生产毫克量的生物活性哺乳动物糖蛋白提供了一种廉价、便捷的方法。
