On the role of the covalent carbohydrate in the action of ricin

the covalent carbohydrate in the toxic lectin ricin has been modified by periodate treatment, and analysis of the products of this reaction indicates that only mannose residues are oxidized. HeLa cell toxicity, cell-surface binding, inhibition of cell-free protein synthesis, and other properties hav...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-12, Vol.255 (23), p.11098-11101
Main Authors: Simeral, L S, Kapmeyer, W, MacConnell, W P, Kaplan, N O
Format: Article
Language:English
Subjects:
Amino Acids - analysis
Binding Sites
Carbohydrates - analysis
Cell Survival - drug effects
HeLa Cells - drug effects
HeLa Cells - metabolism
Humans
Kinetics
Macromolecular Substances
Mannose - analysis
Periodic Acid
Protein Binding
Protein Biosynthesis - drug effects
Ricin - pharmacology
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Summary:the covalent carbohydrate in the toxic lectin ricin has been modified by periodate treatment, and analysis of the products of this reaction indicates that only mannose residues are oxidized. HeLa cell toxicity, cell-surface binding, inhibition of cell-free protein synthesis, and other properties have been investigated as functions of the number of mannose residues modified. The data indicate an important role for mannose in ricin conformation and in the endocytotic process; however, mannose appears not to be essential for binding the toxin to cells.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)70259-2