A chemical derivative of trypsin, selenotrypsin, was prepared to imita
te glutathione peroxidase (GPX) by converting active serine residues i
n the active site of trypsin into selenocysteines. The strategy for pr
eparation of selenotrypsin contained selective sulfonation by phenylme
thanesulfonyl fluoride and nucleophilic substitution by NaHSe. Selenot
rypsin displayed enzyme activity of GPX, which is 150U/(mol. The kinet
ic properties of selenotrypsin was demonstrated to be similar to that
of native GPX.