Two Phytotoxic Anti-Tumor Proteins: Ricin and Abrin

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منابع مشابه

Polyribosome disaggregation in rat liver following administration of the phytotoxic proteins, abrin and ricin.

As the possible mechanisms of inhibition of protein biosynthesis, it was demonstrated that the toxic proteins abrin and ricin cause the degradation of polyribosomes of rat liver or Ehrlich ascites tumor cells. Abrin and ricin have no direct effect on the structural and functional integrity of polyribosomes but act indirectly by increasing the RNase activity in the postmicrosomal supernatant fra...

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Toxicity and detection of ricin and abrin in beverages.

The oral and intraperitoneal (i.p.) toxicities to female BALB/c mice of ricin and abrin in phosphate-buffered saline (PBS), spring water, apple juice, and half-and-half (only oral) were examined after brief (2 h) and prolonged (11 to 13 days) storage. The ricin and abrin samples prepared in PBS had oral toxicities consistent with those previous studies, indicating oral and i.p. 50% lethal doses...

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The binding of abrin and ricin by Ehrlich ascites tumor cells.

teins on the tumor cells was shown to be specific, pH de pendent, 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 sac charides do not. In the presence of D-galactose, the inhibi tion of protein biosynthesis by ricin does not oc...

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The Histological Changes Produced by Ricin and Abrin Intoxications

The study of the effects of the living pathogenic organisms upon the animal body has been succeeded by an era in which especial attent-ion has been directed to the influence of their soluble products. The researches of Oertel* upon human diphtheria, of Babes t and of Welch and Flexner$ upon the experimental form of the disease, the latter including the effects of the soluble products of the gro...

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The Binding of Abrin and Ricin by Ehrlich Ascites Tumor Cells1

teins on the tumor cells was shown to be specific, pH de pendent, 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 sac charides do not. In the presence of D-galactose, the inhibi tion of protein biosynthesis by ricin does not oc...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1973

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)43990-2