title: Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families.
abstract: 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.
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
authors.forename: Jiraporn
authors.initials: J
authors.lastname: Nawarak
authors.forename: Suree
authors.initials: S
authors.lastname: Phutrakul
authors.forename: Shui-Tein
authors.initials: ST
authors.lastname: Chen
mesh_terms: D000818:Animals; D001483:Base Sequence; D030562:Databases, Protein; D017815:Elapidae / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D016650:Fluorescein-5-isothiocyanate / Q000737:chemistry; D006031:Glycosylation; D037102:Lectins / Q000032:analysis*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D020543:Proteome; D011952:Receptors, Concanavalin A / Q000032:analysis / Q000737:chemistry*; D012910:Snake Venoms / Q000032:analysis*; D017819:Viperidae / Q000378:metabolism
chemical_list: D037102:Lectins; D020543:Proteome; D011952:Receptors, Concanavalin A; D012910:Snake Venoms; C027774:concanavalin A-binding glycoproteins; D016650:Fluorescein-5-isothiocyanate