Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Using a micro-organism to make a protein or polypeptide
Patent
1994-02-07
1995-05-09
Lilling, Herbert J.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Using a micro-organism to make a protein or polypeptide
435 691, 435 711, 435196, 435244, 435822, 435849, 435232, C12P 2100, C12P 104, C12N 988
Patent
active
054139201
ABSTRACT:
A method for enhanced production and recovery of phosphate starvation inducible (PSI) gene products. A bacterium having C-P lyase activity is cultured using phosphonate or phosphite (or their mixtures) as the predominant phosphorus source for growth so as to enhance PSI gene product accumulation. PSI gene product is then recovered.
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Gray et al., Periplasmic Production of Correctly Processed Human Growth Hormone in Escherichia coli: Natural and Bacterial Signal Sequences are Interchangeable, Gene, vol. 39, pp. 247-254 (1985).
Wanner, Novel Regulator Mutants of the Phosphate Regulon in Escherichia coli K-12 J. Mol. Biol. vol. 191, pp. 39-58 (1986).
Wanner et al., Phosphate-controlled Gene Expression in Escherichia coli Using Mudl-directed lacZ Fusions, J. Mol. Biol. vol. 158, pp. 347-363 (1983).
Metcalf et al., Involvement of the Escherichia coli phn (psiD) Gene Cluster in Assimilation of Phosphorus in the Form of Phosphonates, Phosphate, Pi esters, and Pi, J. Bacteriol. vol. 173, pp. 587-600 (1991).
Murata, et al., A Microbial Carbon-Phosphorous Bond Cleavage Enzyme Requires Two Protein Components for Activity, J. Bacteriol vol. 171, pp. 4504-4506 (1989).
Wackett et al., Involvement of the Phosphate Regulon and the psiD Locus in the Carbon-Phosphorus Lyase Activity of Escherichia coli K-12, J. Bacteriol. vol. 169, pp. 1753-1756.
Wanner et al., Mapping and Molecular Cloning of phn (psiD) Locus for Phosphonate Utilization in Escherichia coli, J. Bacteriol. vol. 172, pp. 1186-1196 (1990).
Lee Ki-Sung
Metcalf William W.
Wanner Barry L.
Lilling Herbert J.
Purdue Research Foundation
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