Borys M C, Linzer D I, Papoutsakis E T
Department of Chemical Engineering, Northwestern University, Evanston, IL 60208.
Biotechnology (N Y). 1993 Jun;11(6):720-4. doi: 10.1038/nbt0693-720.
Glycosylation patterns and specific expression rates of the recombinant protein mouse placental lactogen-I (mPL-I) by Chinese hamster ovary (CHO) cells varied significantly over the extracellular pH (pHe) range of 6.1 to 8.7. The maximum specific mPL-I expression rates occurred between pHe 7.6 and 8.0. The pHe effect on protein expression was confirmed using a different CHO cell expressing the unglycosylated recombinant protein mouse placental lactogen-II (mPL-II). Decreases in the extent of glycosylation of mPL-I were observed at low (below 6.9) and high (above 8.2) pHe values. The pHe dependent variations in mPL-I accumulation in the supernatant as well as in glycosylation patterns were not the result of enzymatic degradation in the culture medium.
中国仓鼠卵巢（CHO）细胞表达的重组蛋白小鼠胎盘催乳素-I（mPL-I）的糖基化模式和特定表达率在细胞外pH（pHe）6.1至8.7范围内有显著差异。最大特定mPL-I表达率出现在pHe 7.6至8.0之间。使用表达未糖基化重组蛋白小鼠胎盘催乳素-II（mPL-II）的不同CHO细胞证实了pHe对蛋白质表达的影响。在低（低于6.9）和高（高于8.2）pHe值下观察到mPL-I糖基化程度降低。上清液中mPL-I积累以及糖基化模式中pHe依赖性变化并非培养基中酶促降解的结果。
