Abstract
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 (rehLF) is produced at levels up to 5 μg/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.
Original language | English (US) |
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Pages (from-to) | 219-223 |
Number of pages | 5 |
Journal | Gene |
Volume | 122 |
Issue number | 1 |
DOIs | |
State | Published - Dec 1 1992 |
Keywords
- Recombinant DNA
- alcA promoter
- filamentous fungi
- functional assay
- iron-binding glycoprotein
- secretion
ASJC Scopus subject areas
- Genetics