Comparison of thioltransferase (glutathione:disulfide oxidoreductase) from various rat tissues.

Thioltransferase activity was detected in kidney, heart, epididymal fat pads and skeletal muscles, and was inhibited at high concentrations (greater than 1.6 mmol/l) of reduced glutathione. With several disulfide substrates the Vmax and Km for thioltransferase in kidney, heart, soleus and extensor digitorum longus were considerably smaller than in liver. The enzyme from tibialis anterior showed similar kinetic constants as from liver with certain substrates but not with L-cystine.