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• W2023376582 abstract "Macromolecular-translocation inhibitors (MTI) of binding of the activated glucocorticoid-receptor complex (GRC) to nuclei from rat liver are separated into at least three components (MTI-I-III) by DEAE-cellulose column chromatography [Okamoto, K., Isohashi, F., Horiuchi, M. & Sakamoto, Y. (1982) Biochem. Biophys. Res. Commun. 108, 1655-1660]. In this study, we have purified MTI-III from the livers of adrenalectomized rats to apparent homogeneity, as determined by SDS/PAGE. The purification procedure consisted of DEAE-cellulose chromatography, acid treatment and sequential chromatographies using gel filtration, S-Sepharose and Mono S columns. The purified protein had a molecular mass of approximately 69 kDa, as estimated by SDS/PAGE, and the molecular mass of the inhibitor was approximately 68 kDa, as estimated by gel filtration. Thus, MTI-III exerts its inhibitory activity as a monomer. The sedimentation coefficient of MTI-III was approximately 3.7 S. Purified MTI-III was fairly stable at 4 degrees C but at higher temperatures, especially above 25 degrees C, it was rapidly inactivated. Under low-salt conditions, MTI-III was associated with activated GRC (4.2 S) and the resulting complex was detected on sucrose density gradients as a larger species (6.8 S). Initial treatment of nuclei or DNA-cellulose with MTI-III did not alter their abilities to bind activated GRC. These results indicate that MTI-III acts through an interaction with GRC." @default.
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• W2023376582 date "1993-12-01" @default.
• W2023376582 modified "2023-10-16" @default.
• W2023376582 title "Purification and characterization of a macromolecular-translocation inhibitor III of activated glucocorticoid-receptor-complex binding to nuclei from rat liver" @default.
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• W2023376582 doi "https://doi.org/10.1111/j.1432-1033.1993.tb18422.x" @default.
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