Fatty acid synthetase, malic enzyme and other NADP+ binding dehydrogenases have similar antigenic determinant(s) at the NADPH binding domain.
Rabbit IgG prepared against malic enzyme inhibits pigeon liver fatty acid synthetase activity. By screening a number of polyclonal antibodies raised to several dehydrogenases, we have discovered that there is a direct relationship between this cross-reactivity and the existence of a common structural domain whose function is the binding of NADP+/NADPH. The presence of NADP+/NADPH in small concentrations protects against this immunoinhibition, thereby indicating a competitive binding of nucleotide and site-specific antibody at the antigenic domain. These data provide further support for the existence of an antigenic domain in the NADPH binding region of dehydrogenases which is responsible for the production of NADPH site-specific antibodies in polyclonal antisera.
D000818:Animals; D001666:Binding Sites, Antibody; D010856:Columbidae; D000939:Epitopes / Q000302:isolation & purification*; D064429:Fatty Acid Synthases / Q000276:immunology*; D007120:Immunochemistry; D008099:Liver / Q000201:enzymology; D008291:Malate Dehydrogenase / Q000276:immunology*; D008297:Male; D009249:NADP / Q000378:metabolism*; D010088:Oxidoreductases / Q000276:immunology*; D011817:Rabbits
D000939:Epitopes; D009249:NADP; D010088:Oxidoreductases; D008291:Malate Dehydrogenase; D064429:Fatty Acid Synthases