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Optimization of the Expression of Recombinant Human Activin A in the Yeast Pichia pastoris

机译：重组人激活素A在酵母毕赤酵母中表达的优化

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摘要

We report a new procedure to express recombinant human activin A using the methanolic yeast, Pichia pastoris. Optimization of culture procedures has involved comprehensive examination of the effects of culture vessel shape, volume of broth in the induction and expression cultures, methanol concentration, culturing temperature, and pH of the expression cultures. After this optimization, as well as modification of the native cleavage sites, a laboratory scale procedure has been established which routinely produced 2-10 mg/L amounts of this vital growth factor in the highly efficient, eukaryotic yeast system. This system avoids the need to produce this protein and similar TGF-β proteins in mammalian cell lines which, in addition to being costly, produce many native binding partners of these cystine knot proteins, a factor which can dramatically affect yields of the target protein.
机译：我们报告了一种新的程序来表达使用甲醇酵母，毕赤酵母重组人类激活素A。培养程序的优化涉及全面检查培养容器的形状，诱导和表达培养物中的肉汤量，甲醇浓度，培养温度和表达培养物的pH的影响。在优化之后，以及对天然切割位点的修饰，已经建立了实验室规模的程序，该程序通常在高效的真核酵母系统中产生2-10 mg / L的这种重要生长因子。该系统避免了在哺乳动物细胞系中产生这种蛋白质和类似的TGF-β蛋白质的需要，该哺乳动物细胞系除了昂贵之外，还产生这些胱氨酸结蛋白质的许多天然结合伴侣，这可以极大地影响靶蛋白质的产量。

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