CHANGES OF THE HUMAN ERYTHROCYTE-MEMBRANE PROTEIN SH BINDING-SITE PROPERTY WITH EXPOSURE TO FLUORIDE AND 3 STRONG MUTAGENS

The effects of three strong mutagens (potassium bichromate, mitomycin C, and colchicine) and fluoride on the human erythrocyte membrane prot ein SH binding site property have been studied by using the maleimide nitroxide-ESR technique. The results indicate that in singular and com bined treatments with mutagens, the ratio of weakly to strongly immobi lized components is reduced, so that the conformation of the weakly im mobilized component protein is altered. It is possible that the inhibi tion in the cytogenetic response is induced by the interaction of fluo ride with the other chemicals. There is a dose and temperature depende nce of both the singular and the combined action of the mutagen on the membrane protein.