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Tong Q, Yang YG, Zhang HT, et al. The Thioredoxin Reductase-deficient E.coli Mutant Enhances Expression into Solution of Recombinant Proteins Containing Cys Residues. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(1):30-34
Tong, Q., Yang, Y. G., Zhang, H. T., Chen, Y., Yang, S. L., & Gong, Y. (2001). The Thioredoxin Reductase-deficient E.coli Mutant Enhances Expression into Solution of Recombinant Proteins Containing Cys Residues. Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica, 33(1), 30-34.
Tong, Qin, et al. "The Thioredoxin Reductase-deficient E.coli Mutant Enhances Expression into Solution of Recombinant Proteins Containing Cys Residues." Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica vol. 33,1 (2001): 30-34.
Tong Q, Yang YG, Zhang HT, Chen Y, Yang SL, Gong Y. The Thioredoxin Reductase-deficient E.coli Mutant Enhances Expression into Solution of Recombinant Proteins Containing Cys Residues. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(1):30-34. PMID: 12053185.
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Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(1):30-34.

The Thioredoxin Reductase-deficient E.coli Mutant Enhances Expression into Solution of Recombinant Proteins Containing Cys Residues.

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

Qin Tong, Yun-Gui Yang, Hui-Tang Zhang, Yan Chen, Sheng-Li Yang, Yi Gong

Affiliations

  1. Shanghai Research Center of Biotechnology, Chinese Academy of Sciences, Shang hai 200233, China. [email protected]

PMID: 12053185

Abstract

A 3D artificial protein, a salmon calcitonin hexa-polymer, a salmon calcitonin octo-polymer and a human prourokinase, was expressed in the cytoplasma of E.coli GJ980(trxB(-)) mutant. These recombinant proteins containedcysteine residues of different length ranging from 12-22 residues. The mutation was mapped to the gene for thioredoxin reductase(trxB) and was found to eliminate the activity of this enzyme, which was thought to contribute to the sulfhydryl reducing potential of the cytoplasm. Recombinant salmon calcitonin hexapolymer, salmon calcitonin octo-polymer and human prourokinase had more soluble form in cytoplasm of GJ980 mutants than in wild-type strain, while 3D-protein, which has nocysteine residue, still remain in insoluble form. Results indicate the GJ980(trxB(-)) strain allowed the formation of disulphide bonds in the cell cytoplasm which is believed to encourage correct folding and soluble expression of the recombinant proteins.

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