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Comparison of the microsomal NADPH-cytochrome c reductase activities in the four Tetrahymena cells (pyriformis, strain GL and NT-1; thermophilia; ISO) and rat liver was studied. The reductase activity in strain NT-1 was lowest among four Tetrahymena cells grown at 24 degrees C. Rabbit antibody was prepared against the purified NADPH-cytochrome c reductase from Tetrahymena pyriformis (strain NT-1) microsomes. Microsomal NADPH-cytochrome c reductase activities in various Tetrahymena cells were inhibited in proportion to the amount of antibody added, in the order of GL greater than NT-1 greater than thermophilia greater than ISO. No inhibition of reductase activity by antibody was observed in rat liver microsomes.
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