Hepatic microsomal NADPH-cytochrome P-450 reductase was solubilized from rabbit liver microsomes in the presence of detergents and purified to homogeneity by column chromatography. The purified reductase had a molecular weight of 78 000 and contained 1 mol each of FAD and FMN per mol of enzyme. On reduction with NADPH in the presence of molecular oxygen, an 02-stable semiquinone containing one flavin free radical per two flavins was formed, in agreement with previous work on purified trypsin-solubilized reductase. The reduction of oxidized enzyme by NADPH, and autoxidation of NADPH-reduced enzyme by air, proceeded by both one-electron equivalent and two-electron equivalent mechanisms. The reductase reduced cytochrome P-450 (from phenobarbital-treated rabbits) and cytochrome P-448 (from 3-methylcholanthrene-treated rabbits). The rate of reduction of cytochrome P-450 increased in the presence of a substrate, benzphetamine, but that of cytochrome P-448 did not.

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Lactose powder consisting of α-D-lactose monohydrate and anhydrous β-D-lactose was nondestructively and quantitatively evaluated by transmission-type Terahertz time-domain spectroscopy (THz-TDS). An absorption with peak at 39.7 cm −1 (1.19 THz) was assigned to be derived from anhydrous β-D-lactose, in addition to the absorptions due to α-Dlactose monohydrate with peak at 17.1 cm −1 (0.53 THz) and 45.6 cm −1 (1.37 THz). After deconvolution of the spectra using Lorentzian, integrated intensities of the absorptions with peak at 39.7 cm −1 and 45.6 cm −1 were uniquely dependent on the weight composition ratio of the α-and β-lactose powder. As a result, the net molar-ratio of the α-and β-lactose in lactose powder could be precisely evaluated by the integrated intensity ratio. Further, anomer content in lactose powder extracted from lactose solution was evaluated and the refined and unrefined features were shown by the evaluation method.