Enhanced Expression of Human Pro-urokinase cDNA in Escherichia coli(Biological Chemistry)
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概要
- 論文の詳細を見る
Human pro-urokinase cDNA was isolated from the cDNA library constructed from human kidney mRNA using the dC/dG homopolymer tailing method and Okayama-Berg method with pBR322 as a vector. A mature polypeptide starting with Ser was produced in Escherichia coli under the control of the tac promoter and the Shine-Dalgarno sequence of the catechol 2,3-oxygenase gene derived from Pseudomonas putida. By replacing the sequence coding for N-terminal eight amino acids of pro-urokinase with the synthetic DNA oligomer, the bacterial pro-urokinase had a molecular weight of 47,000 daltons and accounted for 15% of the insoluble fraction of E. coli proteins in induced cells. Its biological activity was restored by renaturing the bacterial product. The activity of bacterial pro-urokinase was 450IU/ml culture.
- 社団法人日本農芸化学会の論文
- 1988-02-23
著者
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Hibino Yasuo
Sagami Chemical Research Center
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Miyake Toshio
Sagami Chemical Research Center
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Numao Naganori
Sagami Chemical Research Center
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KONDO Kiyosi
Sagami Chemical Research Center
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OHMORI Muneki
Sagami Chemical Research Center
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MIKI Tetsuzo
Sagami Chemical Research Center
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Matsumoto Reiko
Sagami Chemical Research Center
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KOBAYASHI Yoh-ichi
Sagami Chemical Research Center
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