Elucidation of conservative elements of calmodulin-dependent enzymes with the use of monoclonal antibodies |
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Authors: | N N Alakhov VYu Y" >Modyanov,M I Shakhparonov,E I Zvaritch,M S Feschenko,S V Lutzenko |
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Affiliation: | Institute of Applied Molecular Biology, USSR Ministry of Health, Moscow. |
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Abstract: | Monoclonal antibodies against human erythrocyte membrane Ca2+-ATPase were obtained. The binding of monoclonal antibodies to the enzyme resulted in a decrease in the enzyme sensitivity to calmodulin (CaM). The effects of monoclonal antibodies on other CaM-dependent enzymes, namely, on the phosphodiesterase of cAMP, phosphorylase kinase, and Ca2+-CaM-dependent protein kinase II (PK II), were studied. It was found that all four enzymes contain a common antigenic site. However, the inhibitory effect of antibodies was observed only with respect to Ca2+-ATPase and PK II. The kinetics of the binding of monoclonal antibodies and their inhibitory action were investigated. It was shown that the antigenic site is confined to the calmodulin-binding portion of Ca2+-ATPase and PK II. |
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