Solubilization of the binding protein from Ehrlich ascites cells and erythrocytes to Pseudomonas aeruginosa cytotoxin.

Abstract

The binding protein for pore-forming Pseudomonas aeruginosa cytotoxin was solubilized from Ehrlich ascites cell plasma membranes and rabbit and bovine erythrocyte ghosts using nonionic and zwittergent detergents. Analysis of solubilized plasma membranes from Ehrlich cells by a ligand-blot technique after separation by SDS-PAGE/electrophoretic transfer to nitrocellulose or affinity chromatography showed a protein of 70 kDa molecular mass, which binds to cytotoxin. The binding protein solubilized from rabbit erythrocyte ghosts showed a molecular mass of 50 kDa and that from bovine ghosts 55 kDa according to the former test. The binding proteins could be characterized as acidic. They contain a glycan moiety which is, however, not involved in the interaction of cytotoxin with the binding site.

• Authors: R Jungblut, M Grimmig, R Leidolf, F Lutz
• Journal: Biological chemistry Hoppe-Seyler (Biol Chem Hoppe Seyler) Vol. 373 Issue 2 Pg. 93-100 (Feb 1992) ISSN: 0177-3593 [Print] Germany
• PMID: 1571112 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Bacterial Toxins
• Carrier Proteins
• Detergents
• Exotoxins
• Pseudomonas exotoxin binding protein, mouse
• Receptors, Cell Surface
• Receptors, Cholinergic
• Virulence Factors
• ADP Ribose Transferases
• Pseudomonas aeruginosa exotoxin A

Topics

• ADP Ribose Transferases
• Animals
• Bacterial Toxins
• Carcinoma, Ehrlich Tumor (metabolism)
• Carrier Proteins
• Cattle
• Cell Membrane (metabolism)
• Chromatography, Affinity
• Detergents
• Electrophoresis, Polyacrylamide Gel
• Erythrocyte Membrane (metabolism)
• Exotoxins (metabolism)
• Isoelectric Focusing
• Molecular Weight
• Pseudomonas aeruginosa
• Rabbits
• Receptors, Cell Surface
• Receptors, Cholinergic (isolation & purification, metabolism)
• Solubility
• Virulence Factors