The effects of the site-directed removal of N-glycosylation sites from beta-1,4-N-acetylgalactosaminyltransferase on its function.

@article{Haraguchi1995TheEO,
  title={The effects of the site-directed removal of N-glycosylation sites from beta-1,4-N-acetylgalactosaminyltransferase on its function.},
  author={Masashi Haraguchi and Shigeko Yamashiro and Koichi Furukawa and Kogo Takamiya and Hiroshi Shiku},
  journal={The Biochemical journal},
  year={1995},
  volume={312 ( Pt 1)},
  pages={
          273-80
        }
}
The amino acid sequence deduced from the cloned human cDNA of beta-1,4-N-acetylgalactosaminyltransferase (GalNAc-T; EC 2.4.1.92) gene predicted three potential sites for N-linked glycosylation. Although many glycosyltransferases isolated contain from 2 to 6 N-glycosylation sites, their significance has not been adequately demonstrated. To clarify the roles of N-glycosylation in GalNAc-T function, we generated a series of mutant cDNAs, in which some or all of the glycosylation recognition sites… CONTINUE READING
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