The substrate specificity of the snail Lymnaea stagnalis UDP- G1cNac: G1cNacß-R ß4-N-acetyglucosaminyltransferase reveals a novel variant pathway of complex-type oligosaccharide synthesis

H. Bakker; P.S. Schoenmakers; C.A.M. Koeleman; D.H. Joziasse; I.M. van Die; D.H. van den Eijnden

doi:10.1093/glycob/7.4.539

The substrate specificity of the snail Lymnaea stagnalis UDP- G1cNac: G1cNacß-R ß4-N-acetyglucosaminyltransferase reveals a novel variant pathway of complex-type oligosaccharide synthesis

H. Bakker, P.S. Schoenmakers, C.A.M. Koeleman, D.H. Joziasse, I.M. van Die, D.H. van den Eijnden

VU University medical center

Research output: Contribution to journal › Article › Academic › peer-review

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Original language	English
Pages (from-to)	539-348
Journal	Glycobiology
Volume	7
DOIs	https://doi.org/10.1093/glycob/7.4.539
Publication status	Published - 1997

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10.1093/glycob/7.4.539

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Bakker, H., Schoenmakers, P. S., Koeleman, C. A. M., Joziasse, D. H., van Die, I. M., & van den Eijnden, D. H. (1997). The substrate specificity of the snail Lymnaea stagnalis UDP- G1cNac: G1cNacß-R ß4-N-acetyglucosaminyltransferase reveals a novel variant pathway of complex-type oligosaccharide synthesis. Glycobiology, 7, 539-348. https://doi.org/10.1093/glycob/7.4.539

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The substrate specificity of the snail Lymnaea stagnalis UDP- G1cNac: G1cNacß-R ß4-N-acetyglucosaminyltransferase reveals a novel variant pathway of complex-type oligosaccharide synthesis. / Bakker, H.; Schoenmakers, P.S.; Koeleman, C.A.M. et al.

In: Glycobiology, Vol. 7, 1997, p. 539-348.

Research output: Contribution to journal › Article › Academic › peer-review

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AU - Schoenmakers, P.S.

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