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• W994970986 abstract "This chapter discusses the measurement of substrate and inhibitor binding to microsomal cytochrorne P-450 by optical-difference spectroscopy. Difference spectra are very readily obtained upon addition of numerous foreign chemicals to microsomal preparations. Difference spectra have been found with a variety of characteristics. These were initially classified into three groups, which were (1) a type I spectral change characterized by a peak at about 385 nm and a trough at about 420 nm, (2) a reverse-type I spectral change, which is the mirror image of the type I spectral change, and (3) a type II spectral change characterized by a broad trough between 390 and 410 nm and a peak varying between 425 and 435 nm. It is apparent that careful correlation of inhibitor difference spectra with their effect on metabolism kinetics may distinguish three modes of action, which are (1) binding to oxidized cytochrome P- 450—for example, benzoflavone; (2) binding to reduced cytochrome P-450, for example, ethyl isocyanide, and (3) binding of a reaction produced to reduced cytochrome P-450,for example, SKF-525A." @default.
• W994970986 created "2016-06-24" @default.
• W994970986 creator A5003497148 @default.
• W994970986 date "1978-01-01" @default.
• W994970986 modified "2023-10-17" @default.
• W994970986 title "[27] Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy" @default.
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• W994970986 doi "https://doi.org/10.1016/s0076-6879(78)52029-6" @default.
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