Three thyroxine haptens were synthesized by protecting amino group of thyroxine with Cu 2+ ion and characterized by 1H NMR, MS, elemental analysis and IR. Thyroxine and the derivatives were coupled with carrier protei...Three thyroxine haptens were synthesized by protecting amino group of thyroxine with Cu 2+ ion and characterized by 1H NMR, MS, elemental analysis and IR. Thyroxine and the derivatives were coupled with carrier proteins(BSA and Ovalbumin). Thus antigens were prepared and hapten quantities of the antigens were measured by UV spectroscopy at 320 nm. An anti O methyl T 4 monoclonal antibody was prepared by immunization, cell fusion and screening.展开更多
The abzyme with deiodinase activity was modified with diethyl pyrocarbonate(DEPC) and carbodiimide(EDC) respectively. The modified abzymes were dialyzed and their activities were compared with that of the native abzym...The abzyme with deiodinase activity was modified with diethyl pyrocarbonate(DEPC) and carbodiimide(EDC) respectively. The modified abzymes were dialyzed and their activities were compared with that of the native abzyme. The results indicate that the histidine residue is one of the essential groups in the abzyme, and the modification causes the catalytic activity a loss of 70%. The modification of the residues containing carboxyl group with EDC leads to a loss of 50% activity, indicating that acid amino residues play important roles in the catalytic reaction.展开更多
文摘Three thyroxine haptens were synthesized by protecting amino group of thyroxine with Cu 2+ ion and characterized by 1H NMR, MS, elemental analysis and IR. Thyroxine and the derivatives were coupled with carrier proteins(BSA and Ovalbumin). Thus antigens were prepared and hapten quantities of the antigens were measured by UV spectroscopy at 320 nm. An anti O methyl T 4 monoclonal antibody was prepared by immunization, cell fusion and screening.
文摘The abzyme with deiodinase activity was modified with diethyl pyrocarbonate(DEPC) and carbodiimide(EDC) respectively. The modified abzymes were dialyzed and their activities were compared with that of the native abzyme. The results indicate that the histidine residue is one of the essential groups in the abzyme, and the modification causes the catalytic activity a loss of 70%. The modification of the residues containing carboxyl group with EDC leads to a loss of 50% activity, indicating that acid amino residues play important roles in the catalytic reaction.
