Abstract
The endo-β-N-acetylglucosaminidase mutant endo-CC N180H transfers glycan from sialylglycopeptide (SGP) to various acceptors. The scope and limitations of low-molecular-weight acceptors were investigated. Several homogeneous glycan-containing compounds, especially those with potentially useful labels or functional moieties, and possible reagents in glycoscience were synthesized. The 1,3-diol structure is important in acceptor molecules in glycan transfer reactions mediated by endo-CC N180H as well as by endo-M-N175Q. Glycan remodelling of antibodies was explored using core-fucose-deficient anti-CCR4 antibody with SGP and endo-CC N180H. Homogeneity of the glycan in the antibody was confirmed by mass spectrometry without glycan cleavage.
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Manabe, S., Yamaguchi, Y., Abe, J., Matsumoto, K., & Ito, Y. (2018). Acceptor range of endo-β-n-acetylglucosaminidase mutant endo-CC N180H: From monosaccharide to antibody. Royal Society Open Science, 5(5). https://doi.org/10.1098/rsos.171521
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