Production of Biologically Active Recombinant Human Lactoferrin in Aspergillus Oryzae
| Autor: | Gregory S. May, Mairead Duke, Pauline P. Ward, Denis R. Headon, Orla M. Conneely, Jing Y. Lo |
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| Rok vydání: | 1992 |
| Předmět: |
Aspergillus oryzae
Iron Molecular Sequence Data Biomedical Engineering Heterologous Bioengineering Applied Microbiology and Biotechnology Microbiology law.invention law Complementary DNA Gene expression Humans Secretion Amino Acid Sequence Cloning Molecular Promoter Regions Genetic chemistry.chemical_classification Base Sequence biology Lactoferrin food and beverages DNA biology.organism_classification Recombinant Proteins Blotting Southern Oligodeoxyribonucleotides Biochemistry chemistry biology.protein Recombinant DNA Molecular Medicine alpha-Amylases Glycoprotein Plasmids Biotechnology |
| Zdroj: | Nature Biotechnology. 10:784-789 |
| ISSN: | 1546-1696 1087-0156 |
| Popis: | We report the production of recombinant human lactoferrin in Aspergillus oryzae. Expression of human lactoferrin (hLF), a 78 kD glycoprotein, was achieved by placing the cDNA under the control of the A. oryzae alpha-amylase promoter and the 3' flanking region of the A. niger glucoamylase gene. Using this system, hLF is expressed and secreted into the growth medium at levels up to 25 mg/l. The recombinant lactoferrin is indistinguishable from human milk lactoferrin with respect to its size, immunoreactivity, and iron-binding capacity. The recombinant protein appears to be appropriately N-linked glycosylated and correctly processed at the N-terminus by the A. oryzae secretory apparatus. Lactoferrin is the largest heterologous protein and the first mammalian glycoprotein expressed in the Aspergillus system to date. Hence, this expression system appears suitable for the large-scale production and secretion of biologically active mammalian glycoproteins. |
| Databáze: | OpenAIRE |
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