Enzymatic transfer of sialic acids modified at C-5 employing four different sialyltransferases
We present kinetic studies on the enzymatic transfer of several synthetic sialic acid analogues, modified at C-5, to distinct glycoprotein glycans by sialytransferases differing in acceptor- and linkage-specificity. Biochemical properties of sialic acids were modified by introducing formyl-, trifluo...
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| Main Authors: | , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
December 1995
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| In: |
Glycoconjugate journal
Year: 1995, Volume: 12, Issue: 6, Pages: 739-746 |
| ISSN: | 1573-4986 |
| DOI: | 10.1007/BF00731233 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/BF00731233
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| Author Notes: | H.J. Groß, R. Brossmer |
| Summary: | We present kinetic studies on the enzymatic transfer of several synthetic sialic acid analogues, modified at C-5, to distinct glycoprotein glycans by sialytransferases differing in acceptor- and linkage-specificity. Biochemical properties of sialic acids were modified by introducing formyl-, trifluoroacetyl-, benzyloxycarbonyl-, and aminoacetyl-groups to the amino group at C-5 of neuraminic acid. The latter substitution renders the corresponding α-glyocoside resistant towards sialidases. The respective CMP-sialic acid analogues were prepared by CMP-sialic acid synthase with a yield of 13-55%. |
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| Item Description: | Gesehen am 27.06.2024 |
| Physical Description: | Online Resource |
| ISSN: | 1573-4986 |
| DOI: | 10.1007/BF00731233 |