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Bryodin, a ribosome-inactivating protein from the roots of Bryonia dioica L. (white bryony)
- Source :
- Biochemical Journal; December 1986, Vol. 240 Issue: 3 p659-665, 7p
- Publication Year :
- 1986
-
Abstract
- Bryodin is a strongly basic (pI greater than or equal to 9.5) glycoprotein (neutral sugar content 6.3%) with Mr 30,000, purified from the roots of Bryonia dioica (white bryony). This protein inhibits protein synthesis by a rabbit reticulocyte lysate with and ID50 (concentration causing 50% inhibition) of 0.12 nM (3.6 ng/ml) and has much less effect on protein synthesis by whole cells, with ID50 values ranging from 46 nM to 2.27 microM (1.4-67 micrograms/ml). Bryodin acts by inactivating ribosomes, with a less-than-equimolar ratio, which suggests a catalytic action. Bryodin decreases the number of local lesions induced by tobacco mosaic virus in the leaves of Nicotiana glutinosa. From all its properties, bryodin can be considered to be a ribosome-inactivating protein, similar to those already known [reviews: Barbieri & Stirpe (1982) Cancer Surveys 1, 489-520; Stirpe & Barbieri (1986) FEBS Lett. 195, 1-8].
Details
- Language :
- English
- ISSN :
- 02646021 and 14708728
- Volume :
- 240
- Issue :
- 3
- Database :
- Supplemental Index
- Journal :
- Biochemical Journal
- Publication Type :
- Periodical
- Accession number :
- ejs51299897
- Full Text :
- https://doi.org/10.1042/bj2400659