Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under beta-N-acetylglucosaminidase inhibition.

@article{Watanabe2002SialylationON,
  title={Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under beta-N-acetylglucosaminidase inhibition.},
  author={Satoko Watanabe and Takehiro Kokuho and Hitomi Takahashi and Masashi Takahashi and Takayuki Kubota and Shigeki Inumaru},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 7},
  pages={
          5090-3
        }
}
We investigated the ability of a baculovirus-insect cell system to produce sialylated glycoproteins. Despite the presence of enzymes for synthesizing complex-type N-glycans, the most frequent structure of insect N-glycan is the paucimannosidic type, Man(3)GlcNAc(2)(+/-Fuc). The reason for the overwhelming assembly of paucimannosidic N-glycans is not yet well understood. We hypothesized that this predominance might be due to insect-specific, Golgi-associated beta-N-acetylglucosaminidase… CONTINUE READING
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