Antibodies against alcohol dehydrogenase and lactate dehydrogenase inhibit the activities of other unrelated NADH-requiring dehydrogenases.
Polyclonal rabbit antibodies to NADH-requiring enzymes such as yeast alcohol-dehydrogenase (ADH) and lactate-dehydrogenase (LDH) immunoinhibit the activities of other unrelated dehydrogenases. The immunoinhibition of malate-dehydrogenase (MDH) activity by anti-yeast ADH IgG and anti-hog LDH IgG was dependent on the concentration of antibodies and time. This demonstration of cross-reactivity with unrelated enzyme proteins reveals the existence of an antigenic site around the NADH binding region in each of these enzymes. Pre-treatment of the enzyme with NADH resulted in complete protection against immuno-inactivation. The competitive binding of NADH and the ineffectiveness of ATP establish the difference in the antigenic site around the NADH- and ATP-binding region.
Srivastava
A
A
Department of Chemistry, Indian Institute of Technology, Kanpur.
Katiyar
S S
SS
D000426:Alcohol Dehydrogenase / Q000276:immunology*; D000818:Animals; D000906:Antibodies / Q000276:immunology*; D000937:Antigen-Antibody Reactions; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D007770:L-Lactate Dehydrogenase / Q000276:immunology*; D008291:Malate Dehydrogenase / Q000276:immunology*; D008297:Male; D009247:NADH, NADPH Oxidoreductases / Q000276:immunology*; D011817:Rabbits
D000906:Antibodies; D000426:Alcohol Dehydrogenase; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D009247:NADH, NADPH Oxidoreductases