Aim: To mimic an important family of selenoenzymes in organism-thyroxine (T4) deiodinases and prepare a selenium-containing abzyme catalyzing deiodination of T4.
Methods: A anti-T4 monoclonal antibody was generated by hybridoma methodology and converted into a selenium-containing abzyme by the method of chemical modification. The catalytic activity of the enzyme was measured by RIA method.
Results: The abzyme displayed a marked activity of catalyzing deiodination of T4 and a higher specificity to the substrate T4 than that of natural enzyme, and the double reciprocal plots of the initial rates of T3 formation vs. T4 concentration yielded a family of parallel lines. The catalytic activity could be sensitively inhibited by 6-propyl-2-thiouracil (PTU), a competitive inhibitor for dithiothreitol (DTT).
Conclusion: An abzyme with the diodination activity was first prepared and the reaction mechanism of the enzyme was bisubstrate ping-pong one.