Isolation of antitumor proteins abrin-A and abrin-B from Abrus precatorius.

Two toxic proteins were purified from the seeds of Abrus precatorius by DEAE-A 50 and Sepharose 4B chromatography. One of them does not bind on the Sepharose 4B column (Abrin-b) and the other (Abrin-a) is eluted with 0.2 M galactose. The amino acid compositions and tryptic maps of these two proteins were similar, but not identical. The molecular weights estimated by SDS-gel electrophoresis were 67,000 for abrin-b as compared with 65,000 for abrin-a. In the presence of mercaptoethanol, both abrin-a and abrin-b gave rise to two bands. The lethal doses of abrin-a and abrin-b for mice recorded within 48 h were 10 and 25 microgram per kg of body weight respectively. Abrin-a at 0.8 microgram per ml concentration level agglutinated human 0-type erythrocytes, whereas abrin-b showed no such activity. Abrin-a at 5 microgram per ml concentration level agglutinated both the Sarcoma 180 cells and Ehrlich ascites tumor cells, but it required 150 microgram per ml for abrin-b. Both these two proteins at a sublethal dose could inhibit the growth of Ehrlich ascites tumor cells which were injected simultaneously with these proteins. 131I-abrin-a and 131I-abrin-b were able to bind Sarcoma 180 cells, and the binding of abrin-a could be inhibited by lactose, raffinose, galactose and rhamnose, but none of 15 sugars tested inhibited the binding of abrin-b.