Purification and properties of rat kidney UDP-glucuronosyltransferase
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Substrate specificity of human hepatic Udp-glucuronosyltransferases
2005, Methods in EnzymologyCitation Excerpt :Determination of the substrate specificity of these enzymes has been an important task since the existence of multiple UGT isoforms was proposed (Mulder, 1971) and established through enzyme purification more than 30 years ago (Sanchez and Tephly, 1974). Purification of UGTs from tissue microsomal fractions was (and remains) exceedingly difficult, and the poor retention of functional activity and incomplete separation of the different isoforms prevented a clear description of their substrate specificities (Burchell, 1977; Coughtrie et al., 1987; Weatherill and Burchell, 1980). Cloning and functional expression of individual UGTs in mammalian cell lines some 20 years ago provided the essential systems to define substrate specificity (Fournel‐Gigleux et al., 1991; Jackson et al., 1985).
Physiological modeling of butadiene disposition in mice and rats
2001, Chemico-Biological InteractionsCitation Excerpt :The reported activities of the metabolizing enzymes per milligram of protein were converted into net activities by multiplying by the microsomal or cytosolic protein content of each organ. The activities of P450 and epoxide hydrolase in mice and rats were multiplied by 30, 9, or 9 mg of microsomal protein per gram of tissue for liver [24], lung [25], and kidney [26], respectively. The glutathione S-transferase activities were multiplied by 82.8 or 108 mg of cytosolic protein per gram of tissue for mice and rats, respectively [19].
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