Purification and characterization of glutathione reductase from Chlamydomonas reinhardtii

The purification to homogeneity of glutathione reductase from the unicellular alga Chlamydomonas reinhardtii was carried out. The enzyme was a monomer with a molecular mass of 54-56 kDa computed by gel filtration and SDS-page. The optimum activity was measured at pH 8.2 and 49 degrees centigrade. The enzyme was not specific for NADH, but is specific for NADPH. The immunological characterization of the enzyme was studied using antibodies created against spinach and Euglena enzymes.