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Results for “Benzphetamine”

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At least 55 records · Page 3Linked to original sources
PubMed1985

Relation between the structure of benzphetamine analogues and their binding properties to cytochrome P-450 LM2.

Twelve substrates of a homologous series of tertiary amines (type I substrates) have been reacted with cytochrome P-450 LM2 incorporated into unilamellar liposomes and in soluble form. The apparent spectral dissociation constants (Ks) of the substrate enzyme complexes and the induced high-spin shifts have been correlated with the electron density of distinct carbon atoms as monitored by 13C-NMR chemical shifts, the solubility of the amines and steric parameters of the substrate molecules. The results obtained led to the conclusion that two different intrinsic properties of the substrates can be discriminated in relation to the substrate-enzyme interaction. A diminished electron density at the nitrogen atom is accompanied by an increased binding affinity. The steric structure of the respective substrate determines its capability to shift the spin equilibrium to the high-spin state. Some characteristics of the active center of the enzyme are derived from the evidenced properties of the substrates.

Animals↗
PubMed1982

NADPH-dependent reduction of cytochrome P-450 in liver microsomes from vitamin C-deficient guinea pigs: effect of benzphetamine.

The effect of dietary vitamin C on the reduction of cytochrome c and cytochrome P-450 by NADPH-cytochrome P-450 reductase was determined in guinea pig liver microsomes. Acute vitamin C deficiency decreased hepatic microsomal cytochrome P-450 content 21% and the rate of cytochrome P-450 reduction 66% without affecting cytochrome c reduction. However, the vitamin status of the animals did not affect the enhancement in cytochrome P-450 reduction produced by the addition of a type I substrate to the reaction mixture. The results suggest that vitamin C deficiency selectivity affects the transfer of electron from NADPH to cytochrome P-450 and that this effect does not result from a change in the spin state of cytochrome P-450.

Animals↗