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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Adrenocortical pregnenolone binding activity resides with estrogen sulfotransferase.

Cytosol prepared from Chinese hamster ovary (CHO)-K1 cells transfected with guinea pig estrogen sulfotransferase ( EST) cDNA demonstrated high affinity binding activity for pregnenolone as well as 17 beta-estradiol but failed to bind dehydroepiandrosterone or testosterone. In contrast, cytosol prepared from nontransfected CHO-K1 cells did not demonstrate steroid binding activity. Additionally, the binding activity for pregnenolone and 17 beta-estradiol was dependent on the presence of the cofactor adenosine-3',5'-diphosphate. Pregnenolone and 17 beta-estradiol effectively competed with each other for binding. On the other hand, pregnenolone, which was not sulfonated, did not inhibit the sulfonation of 17 beta-estradiol by expressed EST.[1]

References

  1. Adrenocortical pregnenolone binding activity resides with estrogen sulfotransferase. Lee, Y.C., Park, C.S., Komatsu, K., Kwack, J., Strott, C.A. Endocrinology (1995) [Pubmed]
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