[Purification of lectin from perch (Persa fluviatilis L.) roe specific to cellobiose and study of its characteristics].
Two lectins with different carbohydrate specificity were purified from perch (Persa fluviatilis L.) roe (coastal ecological form) by affinity chromatography on ovariomucine H-sepharose from a human ovary cyst. One lectin was eluted by cellobiose and another lectin was eluted by L-fucose. The L-fucose-specific lectin interacted only with L-fucose and its derivatives, but did not interact with cellobiose and salicin. The cellobiose-specific lectin interacted with all the examined carbohydrates, but cellobiose was the best inhibitor. This lectin can be also purified on cellulose as an affinity sorbent. Unlike the L-fucose-specific lectin from perch roe, the cellobiose-specific lectin is less soluble in water-saline solutions. Lectin solubility increases greatly in presence of specific inhibitors, cellobiose, in particular. L-fucose, alpha-methyl-L-fucopyranoside and 4-nitrophenyl-alpha-L-fucopyranoside are equivalent inhibitors for both lectins. According to SDS-PAGE data, the lectins contain two components with molecular weight 12-13 kDa. In solutions, these components form molecules with 50 or 100 kDa (depending on pH). Data obtained from electrophoresis in PAAG in alkaline (pH 8.9) and acidic system (pH 4.3), and SDS-PAGE did not display essential distinctions between these both lectins.
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D000180:Acrylic Resins / Q000737:chemistry; D000818:Animals; D002475:Cellobiose / Q000737:chemistry*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005632:Fructose / Q000737:chemistry; D005643:Fucose / Q000737:chemistry; D037102:Lectins / Q000302:isolation & purification*; D008970:Molecular Weight; D010063:Ovum / Q000737:chemistry*; D010471:Perches; D012995:Solubility
D000180:Acrylic Resins; D037102:Lectins; C016680:polyacrylamide gels; D002475:Cellobiose; D005643:Fucose; D005632:Fructose