Lipoxygenase Inhibitors

Biochem/physiol Actions Cytochrome P450 enzymes are heme containing monooxygenases which are found primarily in the mammalian liver. They catalyze the oxidative metabolism of xenobiotics.

Biochem/physiol Actions Cytochrome P450 enzymes are heme containing monooxygenases which are found primarily in the mammalian liver. They catalyze the oxidative metabolism of xenobiotics.

Biochem/physiol Actions CYP2B6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and

Biochem/physiol Actions CYP2B6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and

Biochem/physiol Actions CYP2B6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and

Biochem/physiol Actions Cytochrome P450 enzymes are heme containing monooxygenases which are found primarily in the mammalian liver. They catalyze the oxidative metabolism of xenobiotics.

Biochem/physiol Actions Cytochrome P450 enzymes are heme containing monooxygenases which are found primarily in the mammalian liver. They catalyze the oxidative metabolism of xenobiotics.

Biochem/physiol Actions Cytochrome P450 enzymes are heme containing monooxygenases which are found primarily in the mammalian liver. They catalyze the oxidative metabolism of xenobiotics.

CYPMPO is a solvent used in electron spin resonance (ESR) free radical spin trapping. One advantage to using CYPMPO is that it shows preference for trapping superoxide and hydroxyl radicals. Studies indicate that ESR trapping of free radicals is

Application Cytochrome c has been used: in the reduction of ferricytochrome c by xanthine oxidase-generated superoxide radicals as an analyte by the single droplet deposition method using MALDI mass spectra as a terminal electron acceptor in the

Application Cytochrome c has been used: in the reduction of ferricytochrome c by xanthine oxidase-generated superoxide radicals as an analyte by the single droplet deposition method using MALDI mass spectra as a terminal electron acceptor in the

Application Cytochrome c has been used: in the reduction of ferricytochrome c by xanthine oxidase-generated superoxide radicals as an analyte by the single droplet deposition method using MALDI mass spectra as a terminal electron acceptor in the