Purification of sialic acid binding protein from saprophytic bacteria by hydrophobic-interaction chromatography on butyl-toyopearl and polymer-coated porous glass
✍ Scribed by Larisa S. Zhigis; Alexander E. Ivanov; Eugenya M. Rapoport; Emma A. Kovalenko; Ekaterina I. Getman; Vitali P. Zubov
- Publisher
- Springer-Verlag
- Year
- 1993
- Tongue
- English
- Weight
- 283 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0951-208X
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✦ Synopsis
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 BaciNus 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 623% of its initial hemagglutinating activity.