Binding of radiolabeled Staphylococcus aureus delta-toxin to human erythrocytes.
The addition f [3H]isoleucine to a chemically defined medium resulted in the production of delta-toxin (DT) with a high specific radioactivity (0.47 microCi/mg). The purified tritium-labeled toxin ([3H]DT) was found to migrate in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a single band with a molecular weight of 1,600. Upon electrofocusing, [3H]DT yielded one major peak (pI = 5.90) and two minor peaks (pI = 5.10, 6.95) of radioactivity. The percentage of [3H]DT associated with pelleted fractions of intact erythrocytes or erythrocyte ghosts remained fairly constant over a 100-fold range of toxin concentrations. Erythrocyte ghosts, however, bound more [3H]DT than did intact erythrocytes when exposed to the same concentration of toxin. Erythrocytes maintained in isotonic sucrose were more susceptible to toxin than erythrocytes suspended in saline, but did not bind more [3H]DT. The binding of [3H]DT to erythrocyte ghosts was found to be temperature dependent from 0 to 20 degrees C but was constant from 20 to 50 degrees C.
D001427:Bacterial Toxins / Q000302:isolation & purification / Q000378:metabolism*; D002474:Cell-Free System; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D007526:Isoelectric Point; D011485:Protein Binding; D013211:Staphylococcus aureus / Q000276:immunology*; D013696:Temperature
D001427:Bacterial Toxins; C025971:staphylococcal delta toxin