Abstract
Antisera were prepared in rabbits against purified rat liver cytochrome b 5 and NADH-cytochrome c reductase, respectively. With the antiserum against cytochrome b 5 , the cytochrome could be precipitated in immunoelectrophoresis from rough and smooth liver microsomal membranes, kidney microsomes and outer mitochondrial membranes. The cytochrome was precipitable from the rough membranes on the 2nd prenatal day, from the smooth membranes on the day of birth and from the kidney microsomes on the 2nd postnatal day. The NADPH-cytochrome c reductase could be precipitated from the rough and smooth membranes and from kidney microsomes by the specific antiserum. It was precipitable from the rough and smooth membranes at birth and from kidney microsomes on the 2nd postnatal day. No NADPH-cytochrome c reductase was found in the mitochondrial membranes. None of the two antisera contained inhibiting antibodies against the catalytic action of the enzyme against which it was directed.
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