Inhibition of monoclonal antibody binding and proteolysis by light-induced phosphorylation of rhodopsin.

Abstract

Light-induced phosphorylation of rhodopsin in bovine rod outer segment disk membranes inhibits the binding of three carboxyl-terminal-specific anti-rhodopsin antibodies and the cleavage of the carboxyl-terminal region of rhodopsin by trypsin and Staphylococcus aureus V-8 protease. Two monoclonal antibodies, rho 3A6 and rho 1C5, which previously have been… (More)

Topics

Cite this paper

@article{Molday1985InhibitionOM, title={Inhibition of monoclonal antibody binding and proteolysis by light-induced phosphorylation of rhodopsin.}, author={Robert S Molday and David Mackenzie}, journal={Biochemistry}, year={1985}, volume={24 3}, pages={776-81} }