Abstract
The Purification of castor been hemagglutinin has been accomplished first by fractional precipitation with ammonium sulfate then, by hydroxyl apatite column chromatography, and finally, by DEAE-cellulose column chromatography. Protein so obtained and referred to as castor bean hemagglutinin, CBH, was revealed to he homogeneous by examination with moving boundary electro phoresis and sedimentation in the ultracentrifuge. The CBH was able to agglutinate 0.2 ml. of a 4% suspension of washed rabbit erythrocytes by its 0.001 μg. N. The absorption spectrum of CBH was consistent with that of a protein.
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