Comparison of the binding of 7,12-dimethylbenz(a)anthracene and estradiol-17 in the calf uterus cytosol |
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| Authors: | C W Heizmann H I Wyss |
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| Affiliation: | 1. School of Pharmaceutical Sciences, Liaoning University, Shenyang 110036, People''s Republic of China;2. Department of Epidemiology, University of Florida, Gainesville, FL 32608, USA;3. Natural Products Pharmaceutical Engineering Technology Research Center of Liaoning Province, Shenyang 110036, People''s Republic of China;1. School of Life Sciences, Faculty of Medicine, Tianjin University, Tianjin 300072, PR China;2. State Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources, Guangxi Normal University, Guilin 541004, PR China;3. Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, Dalian Minzu University, Dalian, Liaoning 116024, PR China |
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| Abstract: | 7,12-Dimethylbenz(a)anthracene (DMBA) binds to proteins in the calf uterus cytosol. These proteins are not identical with the established estradiol-17β(E2) receptors, as shown by density gradient, gel-electrophoresis, displacement experiments, comparison of thermostability, and additional binding of 3H-DMBA after saturation of the E2 receptors. The physical and chemical behaviours of the two protein complexes are very similar. A maximum binding of hormone and DMBA occurs in the 9S-region (density-gradient) and in the anodic region (gel-electrophoresis). Both complexes dissociate into 5S subunits by treatment with heat or KC1. The four criteria for a ‘Receptor’ (hormone specificity, tissue specificity, high affinity and saturation) are not satisfied by the DMBA-binding proteins. |
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