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  • Title: Interaction of the hepatic receptor protein for 2,3,7,8-tetrachlorodibenzo-rho-dioxin with DNA.
    Author: Carlstedt-Duke JM, Harnemo UB, Högberg B, Gustafsson JA.
    Journal: Biochim Biophys Acta; 1981 Jan 21; 672(2):131-41. PubMed ID: 6261827.
    Abstract:
    2,3,7,8-Tetrachlorodibenzo-rho-dioxin (TCDD) binds to a specific, high-affinity, low-capacity protein in rat liver cytosol. The TCDD-receptor complex is a large molecule with a Stokes radius of 6.6 nm as determined by gel filtration on calibrated columns. The receptor complex sediments at 5.0 S on glycerol gradients. The calculated molecular weight from the physical parameters was 136 000 and the frictional ratio 1.79. The TCDD-receptor complex binds to DNA-cellulose without preceding heat activation or incubation at high ionic strength. The receptor must first bind TCDD before it can interact with DNA. The DNA-binding ability can be removed from the TCDD receptor by limited proteolysis with trypsin. This treatment does not affect the TCDD-binding site of the receptor. The proteolytic fragment of the TCDD-receptor complex containing the TCDD-binding site but not the ability to bind to DNA appears to be approximately the same size as the native receptor, as judged from chromatography of Sepharose CL-6B and glycerol gradient centrifugation.
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