TY - JOUR
T1 - The Binding of Abrin and Ricin by Ehrlich Ascites Tumor Cells
AU - Lin, Jung Yaw
AU - Ju, Shyr Te
AU - Wu, Hua Lin
AU - Tung, Ta Cheng
PY - 1973/11
Y1 - 1973/11
N2 - Abrin and ricin cause 50% agglutination of Ehrlich ascites tumor cells (5*106/ml) at a concentration of 8 and 4 μg/ml, respectively. Addition of D-galactose or its derivatives, lactose or raffinose, inhibits the agglutinating activity of the toxic proteins. Binding of 13 I-toxic proteins on the tumor cells was shown to be specific, pH dependent, and concentration dependent. Native ricin, abrin, D-galactose, and its sterically related saccharides inhibit this specific binding, while concanavalin A, bovine serum albumin, heat-denatured abrin or ricin, and other saccharides do not. In the presence of D-galactose, the inhibition of protein biosynthesis by ricin does not occur in vitro.
AB - Abrin and ricin cause 50% agglutination of Ehrlich ascites tumor cells (5*106/ml) at a concentration of 8 and 4 μg/ml, respectively. Addition of D-galactose or its derivatives, lactose or raffinose, inhibits the agglutinating activity of the toxic proteins. Binding of 13 I-toxic proteins on the tumor cells was shown to be specific, pH dependent, and concentration dependent. Native ricin, abrin, D-galactose, and its sterically related saccharides inhibit this specific binding, while concanavalin A, bovine serum albumin, heat-denatured abrin or ricin, and other saccharides do not. In the presence of D-galactose, the inhibition of protein biosynthesis by ricin does not occur in vitro.
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M3 - Article
C2 - 4748430
AN - SCOPUS:0015692508
VL - 33
SP - 2688
EP - 2691
JO - Cancer Research
JF - Cancer Research
SN - 0008-5472
IS - 11
ER -