Analysis of Lectin-Bound Glycoproteins in Snake Venom from the Elapidae and Viperidae Families
| Autor: | Shui-Tein Chen, Suree Phutrakul, Jiraporn Nawarak |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Glycosylation
Proteome Glycoconjugate Molecular Sequence Data complex mixtures Biochemistry Mass Spectrometry Receptors Concanavalin A chemistry.chemical_compound Viperidae Lectins biology.animal Animals Electrophoresis Gel Two-Dimensional Elapidae Databases Protein chemistry.chemical_classification Base Sequence biology Molecular mass Lectin General Chemistry biology.organism_classification Molecular biology chemistry Snake venom biology.protein Glycoprotein Fluorescein-5-isothiocyanate Snake Venoms |
| Zdroj: | Journal of Proteome Research. 3:383-392 |
| ISSN: | 1535-3907 1535-3893 |
| DOI: | 10.1021/pr034052+ |
| Popis: | This paper describes an efficient method of studying the glycoproteins found in snake venom. The glycosylation profiles of the Elapidae and Viperidae snake families were analyzed using FITC-labeled lectin glycoconjugates. The Con A-agarose affinity enrichment technique was used to fractionate glycoproteins from the N. naja kaouthia venom. The results revealed a large number of Con A binding glycoproteins, most of which have moderate to high molecular weights. To identify the proteins, the isolated glycoprotein fractions were subjected to two-dimensional electrophoresis and MALDI-TOF MS. Protein sequences were compared with published protein databases to determine for their biological functions. |
| Databáze: | OpenAIRE |
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