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Elucidation of Conservative Elements of Calmodulin‐Dependent Enzymes with the Use of Monoclonal Antibodies
Author(s) -
Alakhov VYu,
Modyanov NN,
Shakhparonov MI,
Zvaritch EI,
Feschenko MS,
Lutzenko SV
Publication year - 1988
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1988.tb00022.x
Subject(s) - monoclonal antibody , calmodulin , enzyme , phosphodiesterase , biochemistry , chemistry , microbiology and biotechnology , antibody , epitope , phosphorylase kinase , atpase , antigen , glycogen phosphorylase , biology , immunology
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.