抄録
Hemagglutinin was extracted from castor beans and purified by gel filtration on Sephadex G-75 followed by DEAE-cellulose column chromatography. The molecular weight of castor bean hemagglutinin (CBH) was estimated to be 130, 000 by SDS-polyacrylamide gel electrophoresis and its isoelectric point to be 7.8 by isoelectric focusing electrophoresis. CBH possessed the identical N-terminal amino acids (Ile and Ala) and a very similar amino acid composition to those of ricin D, whereas its toxicity for mice was about 1% of that of ricin D.
