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

Autor:	Emma A. Kovalenko, Ekaterina I. Getman, Eugenya M. Rapoport, Alexander E. Ivanov, Vitali P. Zubov, Larisa S. Zhigis
Rok vydání:	1993
Předmět:	Chromatography biology Chemistry Hydrophilic interaction chromatography Lectin Sialic acid binding Bacillus subtilis Porous glass biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Bacillales Sialic acid Hydrophobic effect chemistry.chemical_compound biology.protein
Zdroj:	Biotechnology Techniques. 7:667-670
ISSN:	1573-6784 0951-208X
DOI:	10.1007/bf00151867
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::81b03f414749540665dda57bd113a522 https://doi.org/10.1007/bf00151867 Zobrazit plný text záznamu Full text from SpringerLink