Fast purification of Phaseolus vulgaris isolectins.
Phytohemagglutinin from red kidney bean has been purified by affinity chromatography on a human alpha 1-acid glycoprotein Sepharose 4B column. Further purification of the hemagglutinin's five isolectins was achieved on a Mono S column with an 86% protein recovery. Each sequentially eluted isolectin from the ion exchange column displayed either hemagglutinating or mitogenic activity. The main activity of each fraction was the result of the combination of varying proportions of the L and E subunits.
Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México.
E
E
Zenteno
M
M
Ortega
Z
Z
Qin
J
J
Montreuil
H
H
Debray
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods; D004261:DNA Replication / Q000187:drug effects; D004591:Electrophoresis, Polyacrylamide Gel; D006386:Hemagglutination Tests; D006801:Humans; D037102:Lectins / Q000302:isolation & purification* / Q000494:pharmacology; D051379:Mice; D008938:Mitosis / Q000187:drug effects; D037121:Plant Lectins; D010944:Plants; D012639:Seeds; D012685:Sepharose; D013154:Spleen / Q000166:cytology / Q000187:drug effects
D037102:Lectins; D037121:Plant Lectins; D012685:Sepharose