Binding ofrasp21 to bands 4.2 and 6 of human erythrocyte membranes

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Abstract
The direct binding protein(s) of ras p21 was (were) investigated in inside‐out vesicles of human erythrocyte ghosts using the pure v‐Kirsten (Ki)‐ras p21 synthesized in E. coli. The bound ras p21 was detected immunochemicallly using an anti‐v‐Ki‐ras p21 monoclonal antibody. ras p21 bound to vesicles. Prior digestion of the vesicles with trypsin reduced this binding significantly. When ras p21 was laid over vesicle proteins immobilized on a nitrocellulose sheet by transfer from the gel of SDS‐polyacrylamide gel electrophoresis, ras p21 bound to bands 4.2 and 6. ras p21 binding to these proteins was reduced by prior incubation of ras p21 with the purified band 4.2 or 6 protein. These results indicate that v‐Ki‐ras p21 can bind directly to bands 4.2 and 6 of human erythrocyte membranes as far as tested in an in vitro cell‐free system.