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Ribosomal inactivation

Bhatia, N., McDonald, K. A., Jackman, A. P., and Dandekar, A. M, A simplified procedure for the purification of trichosanthin (a type 1 ribosome inactivating protein) from Trichosanthes kirilowii root tubers, Prot. Purif. Expression, 7, 143, 1996. [Pg.309]

Due to the extraordinary toxicity of intact ribosome-inactivating toxins like ricin, abrin, and modeccin, purification and handling of these proteins must be done with extreme care. Even dust from crude seed powders or lyophilized proteins should be considered dangerous. During... [Pg.828]

Lambert, J.M., Blattler, W.A., McIntyre, G.D., Golmacher, V.S., and Scott Jr., C.F. (1988) Immunotoxins containing single chain ribosome-inactivating proteins. In Immunotoxins (A.E. Frankel, ed.), p. 175. Kluwer, Boston. [Pg.1086]

The antileukemic efficacy of an immunotoxin composed of a monoclonal anti-Thy-1 antibody disulfide linked to the ribosome-inactivating protein gelonin. Cancer Immunol. Immunother. 25, 31. [Pg.1112]

P = constitutive promoter, tetR = TETrepressor gene,TETR = TET repressor protein, tetO = TET operator sequence, = tetracycline, ere/CRE = Cre recombinase gene/protein, PLEA = late embryogenesis abundant promoter, RIP = gene for ribosome inactivating protein, shaded blocks are loxP sites in orientation shown by solid triangle. After [48]... [Pg.261]

Delayed-action cytotoxins that inhibits protein synthesis (ribosomal inactivating protein). They are obtained from the seed of the Jequirity beans plant (Abrus precatorius). Typically yellowish-white powders that are insoluble in distilled water but soluble in salt water. They are fairly heat stable. [Pg.478]

Cytotoxin that inhibits protein synthesis (ribosomal inactivating protein). It is obtained from the roots of Adenia digitata plant. [Pg.481]

Delayed-action cytotoxin that inhibits protein synthesis (ribosomal inactivating protein) that is obtained from castor beans (Ricinus communis). Waste from production of castor oil contains about 5% ricin by weight. It is a white powder that is soluble in water and relatively heat stable. Aqueous solutions are resistant to chlorine at 10 ppm. It is persistent in the environment. [Pg.482]

Ribosome inactivating cytotoxic protein that irreversibly inhibits protein synthesis in cells, causing cell death. It is a solid obtained from bacteria (Shigella dysenteriae). [Pg.483]

Tobacco expressing interleukin-10 is currently being studied as a potential treatment for Crohn s disease. Similarly, trichosanthin (a ribosome inactivator used to inhibit HIV infection) and angiotensin have been expressed in plants. Hirudin (antithrombin) is commercially expressed in plants (Parmenter et al., 1995 Prakash, 1996). [Pg.44]

BOX 29-A THE DIPHTHERIA TOXIN AND OTHER RIBOSOME-INACTIVATING PROTEINS... [Pg.1685]

Lambert, J. M., Senter, P. D., Yau-Young, A., Blattler, W. A., and Goldmacher, V.S. (1985) Purified immunotoxins that are reactive with human lymphoid cells monoclonal antibodies conjugated to the ribosome-inactivating proteins gelonin and the pokeweed antiviral proteins./. Biol. Chem. 260,12035—12041. [Pg.720]


See other pages where Ribosomal inactivation is mentioned: [Pg.297]    [Pg.310]    [Pg.1054]    [Pg.45]    [Pg.219]    [Pg.827]    [Pg.827]    [Pg.829]    [Pg.830]    [Pg.847]    [Pg.1121]    [Pg.481]    [Pg.485]    [Pg.215]    [Pg.213]    [Pg.957]    [Pg.113]    [Pg.89]    [Pg.1668]    [Pg.1844]    [Pg.135]    [Pg.144]    [Pg.154]    [Pg.752]    [Pg.753]    [Pg.517]    [Pg.517]    [Pg.518]    [Pg.518]    [Pg.519]    [Pg.536]   
See also in sourсe #XX -- [ Pg.847 ]

See also in sourсe #XX -- [ Pg.497 , Pg.516 ]

See also in sourсe #XX -- [ Pg.497 , Pg.516 ]




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Ribose Ribosomal-inactivating

Ribosome-inactivating protein abrin

Ribosome-inactivating protein ricin

Ribosome-inactivating proteins

Ribosome-inactivating proteins RIPs)

Ribosome-inactivating proteins Ribosomes

Ribosome-inactivating proteins active site

Ribosome-inactivating proteins plant

Ribosome-inactivating toxins

Ribosome-inactivation protein

Ribosome-inactivation protein toxins

Type I ribosome-inactivating proteins

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