Immunotoxins containing single chain ribosome-inactivating proteins
- 1 January 1988
- book chapter
- Published by Springer Nature
- Vol. 37, 175-209
- https://doi.org/10.1007/978-1-4613-1083-9_12
Abstract
Proteins1 that catalytically inactivate eukaryotic ribosomes have been identified in the extracts of a wide variety of plants [1–3]. Such ribosome-inactivating proteins can be divided into two classes. One class comprises proteins that consist of two nonidentical subunits, each of Mr about 30,000 (A and B chains), that are joined by a disulfide bond [1, 2, 4]. Ricin, which has been known for many years, is the best studied example of this class, which also includes abrin, modeccin, volkensin, and viscumin [3, 4]. The B chains of these proteins have the property of binding to cell-surface carbohydrates and promote the uptake of their A chain into cells [1–4]. Entry of the A chain of these toxins into the cytoplasm of a cell then results in the death of the cell by inactivation of its ribosomes. Members of this class of ribosome-inactivating proteins are extremely cytotoxic for cultured cell lines and are very poisonous for animals.Keywords
This publication has 100 references indexed in Scilit:
- The pharmacokinetics and toxicity of murine monoclonal antibodies and of gelonin conjugates of these antibodiesInternational Journal of Immunopharmacology, 1987
- Ribonuclease activity associated with the 60S ribosome-inactivating proteins ricin A, phytolaccin and Shiga toxinBiochemical and Biophysical Research Communications, 1985
- Characterization of a Saponaria officinalis seed ribosome-inactivating protein: Immunoreactivity and sequence homologiesBiochemical and Biophysical Research Communications, 1985
- The immunological activity of plant toxins used in the preparation of immunotoxins—II. The immunodepressive activity of geloninInternational Journal of Immunopharmacology, 1985
- Dodecandrin, a new ribosome-inhibiting protein from Phytolacca dodecandraBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- The protein synthesis inhibitors from wheat, barley, and rye have identical antigenic determinantsBiochemical and Biophysical Research Communications, 1983
- The immunomodulatory activity of the plant proteins Momordica Charantia inhibitor and Pokeweed antiviral proteinInternational Journal of Immunopharmacology, 1983
- Targeting of the antiviral protein from Phytolaccaamericana with an antibodyBiochemical and Biophysical Research Communications, 1982
- Effect of inhibitors of protein synthesis from plants on tobacco mosaic virus infectionCellular and Molecular Life Sciences, 1981
- Epidermal growth factor-toxin A chain conjugates: EGF-Ricin A is a potent toxin while EGF-diphtheria fragment A is nontoxicCell, 1980