PURIFICATION OF SIALIC-ACID BINDING-PROTEIN FROM SAPROPHYTIC BACTERIABY HYDROPHOBIC-INTERACTION CHROMATOGRAPHY ON BUTYL-TOYOPEARL AND POLYMER-COATED POROUS-GLASS
Ls. Zhigis et al., PURIFICATION OF SIALIC-ACID BINDING-PROTEIN FROM SAPROPHYTIC BACTERIABY HYDROPHOBIC-INTERACTION CHROMATOGRAPHY ON BUTYL-TOYOPEARL AND POLYMER-COATED POROUS-GLASS, Biotechnology techniques, 7(9), 1993, pp. 667-670
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 Bacil
lus subtilis Hydrophobic-interaction chromatography on the Butyl-WPG p
romotes the better resolution of nonactive contaminants from the activ
e lectin. There were found optimal conditions for HPLC-analysis of pur
ified lectin preparations. One step of chromatography on the butyl-WPG
provided a considerable purification of lectin (98% of contaminants w
ere removed), which retained 62,5% of its initial hemagglutinating act
ivity