Purification of sialic acid binding protein from saprophytic bacteria by hydrophobic-interaction chromatography on butyl-toyopearl and polymer-coated porous glass

Two rigid sorbents with identical nominal hydrophobic functions (Butyl-Toyopearl and poly(N-butylacrylamide)-coated porous glass (Butyl-WPG)) were compared upon chromatographic purification of lectin from Bacillus subtilis. Hydrophobic-interaction chromatography on the Butyl-WPG promotes the better resolution of nonactive contaminants from the active lectin. There were found optimal conditions for HPLC-analysis of purified lectin preparations. One step of chromatography on the butyl-WPG provided a considerable purification of lectin (98% of contaminants were removed), which retained 62,5% of its initial hemagglutinating activity.