PURIFICATION OF SIALIC-ACID BINDING-PROTEIN FROM SAPROPHYTIC BACTERIABY HYDROPHOBIC-INTERACTION CHROMATOGRAPHY ON BUTYL-TOYOPEARL AND POLYMER-COATED POROUS-GLASS

Citation
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
Citations number
11
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
0951208X
Volume
7
Issue
9
Year of publication
1993
Pages
667 - 670
Database
ISI
SICI code
0951-208X(1993)7:9<667:POSBFS>2.0.ZU;2-V
Abstract
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