Purification and Properties of Thioredoxin-I from Cryptococcus neoformans

Purification and Properties of Thioredoxin-I from Cryptococcus neoformans

Thioredoxin-I(Trx-I) was partially purified from Cryptococcus neoformans by procedures including heat treatment, DEAE-cellulose ion exchange chromatography, gel filtration on Sephadex G-50, and Q-Sepharose ion exchange chromatography. Its molecular weight is 16.3 kDa protein, which is relatively larger than most known thioredoxins. However, this enzyme is very heat-stable protein. The C. neoformans thioredoxin-I shows a 176-fold lower catalytic efficiency than E. coli thioredoxin when E. coli thioredoxin reductase was used as a reducing enzyme. Further studies should be doe to elucidate the precise role of thioredoxin-I from C. neoformans.