Specificity of the sialic acid-binding lectin from the snail Cepaea hortensis
The specificity of the sialic acid-binding lectin from the snail Cepaea hortensis, purified by affinity chromatography on fetuin-Sepharose, was studied by hemagglutination inhibition assay applying 32 sialic acid derivatives and 14 glycoproteins. 2-alpha-Methyl-9-O-acetyl-NeuAc was the most potent i...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
5 May 1992
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| In: |
The journal of biological chemistry
Year: 1992, Volume: 267, Issue: 13, Pages: 8752-8756 |
| ISSN: | 1083-351X |
| DOI: | 10.1016/S0021-9258(19)50342-8 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/S0021-9258(19)50342-8 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0021925819503428 
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| Author Notes: | Reinhard Brossmer, Manfred Wagner, Edgar Fischer |
| Summary: | The specificity of the sialic acid-binding lectin from the snail Cepaea hortensis, purified by affinity chromatography on fetuin-Sepharose, was studied by hemagglutination inhibition assay applying 32 sialic acid derivatives and 14 glycoproteins. 2-alpha-Methyl-9-O-acetyl-NeuAc was the most potent inhibitor, followed closely by 2-alpha-methyl-NeuAc and 2-alpha-benzyl-NeuAc. An axially orientated carboxyl group is a prerequisite for maximal lectin-sugar binding. Neither size nor polarity of the alpha-anomeric substituent significantly influenced inhibition potency. An intact sialic acid N-acetyl group is essential for optimal lectin-sugar interaction. The trihydroxypropyl side chain also is of great importance. However, a bulky hydrophobic substituent at the side chain like a 9-O-tosyl residue did not decrease binding to the lectin. The lectin did not distinguish between NeuAc alpha 2—-3Gal beta 1—-4Glc and NeuAc alpha 2—-6Gal beta 1—-4Glc. Among other sugars tested, only N-acetylglucosamine showed inhibition, although 50-fold less. The most potent glycoprotein inhibitors were those carrying O-chains only or preferentially, as ovine submaxillary mucin, bovine submaxillary mucin, and glycophorin A. Tamm-Horsfall protein was an exception being a strong inhibitor, although carrying only N-chains. Asialoglycoproteins were inactive. Glycoproteins containing the NeuAc alpha 2—-3Gal sequence inhibited the lectin as well as those with NeuAc alpha 2—-6GalNAc. From the results a model of the lectin's binding site for sialic acid is suggested. |
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| Item Description: | Artikel-Version: 4. Januar 2021 Gesehen am 24.06.2024 |
| Physical Description: | Online Resource |
| ISSN: | 1083-351X |
| DOI: | 10.1016/S0021-9258(19)50342-8 |