ArticleApplied microbiology and biotechnology1991
Expression of human antithrombin III in the cellular slime mould Dictyostelium discoideum.
Article in Applied microbiology and biotechnology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- Optimizing heterologous expression in dictyostelium: importance of 5' codon adaptation.Nucleic acids research · 2000Article
- Analysis of gene function in Dictyostelium.Experientia · 1995Review
- Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells.The Biochemical journal · 1995Article
- Overexpression of myosin motor domains in Dictyostelium: screening of transformants and purification of the affinity tagged protein.Journal of muscle research and cell motility · 1995Article
- Expression of the rotavirus SA11 protein VP7 in the simple eukaryote Dictyostelium discoideum.Journal of virology · 1995Article
- Immobilization of the slime mould Dictyostelium discoideum for the continuous production of recombinant human antithrombin III.Applied microbiology and biotechnology · 1993Article
- Transcriptional regulation by folate: inducible gene expression in Dictyostelium transformants during growth and early development.Nucleic acids research · 1992Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to test the biotechnological potential of the cellular slime mould Dictyostelium discoideum the cDNA coding for human antithrombin III was expressed in this microorganism. The 1392-bp antithrombin III cDNA was fused to the N-terminal coding part of the D. discoideum actin 6 gene. In constructs carrying this artificial N-terminal coding region only low amounts of antithrombin III were detected. However, constructs from which all actin coding nucleotides were removed produced significant amounts of anti-thrombin III, most of which was secreted into the culture broth. Stationary cultures (1.5 x 10(7) cells/ml) of certain stable transformants accumulated up to 1.0 microgram antithrombin III/ml culture medium within 24 h. The recombinant protein has a slightly smaller molecular weight in sodium dodecyl sulphate-polyacrylamide gels than authentic plasma antithrombin III and it is glycosylated, as determined by concanavalin A labelling.
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