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 colu mn. Further purification of the hemagglutinin's five isolectins was ac hieved on a Mono S column with an 86% protein recovery. Each sequentia lly eluted isolectin from the ion exchange column displayed either hem agglutinating or mitogenic activity. The main activity of each fractio n was the result of the combination of varying proportions of the L an d E subunits.