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Production of recombinant endostatin from stably transformed Trichoplusia ni BTI Tn 5B1-4 cells

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Abstract

The recombinant plasmids harboring a heterologous gene coding mouse endostatin were transfected and expressed stably in Trichoplusia ni BTI Tn 5B1-4 (Tn 5B1-4) cells. Recombinant endostatin expressed in the stably transformed Tn 5B1-4 cells was secreted into the medium. Recombinant endostatin was also purified to homogeneity using a simple one-step Ni2+ affinity fractionation method. Purified recombinant endostatin inhibited endothelial cell proliferation in a dose-dependent manner. The concentration at half-maximum inhibition (ED50) for recombinant endostatin was approximately 0.35 μg ml−1. In a T-flask, the stably transformed Tn 5B1-4 cells produced 14.3 mg recombinant endostatin l−1 at 6 days of cultivation.

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Lee, J.M., Chang, K.H., Park, J.H. et al. Production of recombinant endostatin from stably transformed Trichoplusia ni BTI Tn 5B1-4 cells. Biotechnology Letters 23, 1931–1936 (2001). https://doi.org/10.1023/A:1013726113708

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  • DOI: https://doi.org/10.1023/A:1013726113708

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