منابع مشابه
Potent inhibition of human liver aldehyde oxidase by raloxifene.
The selective estrogen receptor modulator, raloxifene, has been demonstrated as a potent uncompetitive inhibitor of human liver aldehyde oxidase-catalyzed oxidation of phthalazine, vanillin, and nicotine-Delta1'(5')-iminium ion, with K(i) values of 0.87 to 1.4 nM. Inhibition was not time-dependent. Raloxifene has also been shown to be a noncompetitive inhibitor of an aldehyde oxidase-catalyzed ...
متن کاملHepatic Aldehyde Oxidase
Previous reports on rabbit liver aldehyde oxidase described the purification and some properties of the enzyme (1) and the differential inhibition of electron transfer to various acceptors (2). The latter study furnished evidence for the participation of several electron carriers in the internal electron transport sequence of the enzyme. The present communication summarizes the results of studi...
متن کاملKinetic studies on protoporphyrinogen oxidase inhibition by diphenyl ether herbicides.
Diphenyl ethers (DPEs) and related herbicides are powerful inhibitors of protoporphyrinogen oxidase, an enzyme involved in the biosynthesis of haems and chlorophylls. The inhibition kinetics of protoporphyrinogen oxidase of various origins by four DPEs, (methyl)-5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid (acifluorfen and its methyl ester, acifluorfen-methyl), methyl-5-[2-chloro...
متن کاملStudies of aldehyde oxidase by electron paramagnetic resonance spectroscopy. II. Kinetic studies by rapid freezing.
Aldehyde oxidase from rabbit liver was studied by electron paramagnetic resonance (EPR) spectroscopy. Reduction by substrate elicited three types of signals characteristic of free radicals, molybdenum(V), and a non-heme iron complex, respectively. The properties of these signals are described, and the representation of each species in the corresponding signal is quantitatively assessed. Under t...
متن کاملStudies on Cytochrome Oxidase
Ever since cytochrome oxidase was first solubilized from heart muscle preparations by Yakushiji and Okunuki (1) and Straub (2) in 1941, the further purification of this enzyme has been the subject of studies by many workers, using extraction with bile salts (3-14), or digestive enzymes such as trypsin (6, 7) and snake venom (15), fractionation with ammonium sulfate (5-14), chromatography (9, 12...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1955
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)71016-8