The purification and properties of aldose reductase from rat ovary
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Purification and characterization of aldose reductase from jerboa (Jaculus orientalis) and evaluation of its inhibitory activity by Euphorbia regis-jubae (Webb & Berth) extracts
2021, Comparative Biochemistry and Physiology Part - C: Toxicology and PharmacologyCitation Excerpt :In the pooled fractions from the Blue Sepharose column, only one protein band was detected using an SDS-PAGE with a molecular weight of 38 ± 1 kDa (Fig. 2a and b). In another study, the purified enzyme from rat ovary exhibited a single protein band with a mobility corresponding to a molecular weight of 39.9 kDa (Iwata et al., 1990). The AR showed maximum activity in jerboa kidneys during prehibernating state.
Isolation of the mouse aldose reductase promoter and identification of a tonicity-responsive element
1997, Journal of Biological ChemistryEffects of psychotropic drugs on aldo-keto reductase activity in rat ovary and adrenal gland
1996, Biochemical PharmacologyAldose reductase is a major reductase for isocaproaldehyde, a product of side-chain cleavage of cholesterol, in human and animal adrenal glands
1996, Archives of Biochemistry and Biophysics
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Present address: Division of Xenobiotic Metabolism and Disposition, National Institute of Hygienic Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158.
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