Abstract
Human fetal liver microsomes were shown to contain the components of the NADPH- and NADH-linked electron transport systems. The NADPH-linked system was capable of hydroxylating testosterone and laurate, but unable to oxidize exogenous substrates such as 3, 4-benzpyrene and aminopyrine. The spectral change associated with the binding of the substrate to cytochrome P-450 was of the type I variety with testosterone and laurate and type II with aminopyrine.
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