NADPH-cytochrome c reductases of Trypanosoma cruzi.
NADPH-dependent reduction of cytochrome c is catalyzed both by microsomes and the cytosolic fraction isolated from Trypanosoma cruzi homogenates. About one-third of the activity is microsomal and two-thirds is cytosolic. The microsomal activity is increased by Lubrol and sodium cholate, but pretreatment with phenobarbital has negligible effect. On the other hand, detergents do not affect the cytosolic activity but it is increased by phenobarbital. From these observations, it is concluded that the NADPH-dependent reduction of cytochrome c by microsomes and the cytosol corresponds to two distinct enzymes. The cytosolic enzyme has been purified to a single SDS-PAGE band of about 53,000 da and partially characterized.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D009251:NADPH-Ferrihemoprotein Reductase / Q000302:isolation & purification / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D014349:Trypanosoma cruzi / Q000201:enzymology*
D009251:NADPH-Ferrihemoprotein Reductase