[Lotus]

Moreover, there is 35% of population that has not the enzimatic process which converts and activate genisteine and daidzeine (they both need to cut off the glycone, to be active), this occurs in the gut.

Ok thanks, (please see related source below).

sorry, i was wrong, the correct pathway is: 35% of population can convert daidzein and genistein to the active compound "equol".
(glycone is cut off by everyone, i think)
i'm sorry but the source is in italian, i didnt find it yet in english:
http://www.iss.it/binary/cnra/cont/ALIME...270810.pdf
(page 18)

The source looks very interesting, sorry....I suck at translations

"What's also interesting is how upon excertion steroids are water soluble"-->
mmh... why do you want to know that? for transport?

Yes exactly, (for transport), ion channels are the access of cell diffusion correct?, assuming carrier proteins are the vehicles to mitochondria, what keeps the channels open long enough expression?, I see its from 1/100 hundredth to 1/1000 thousands of seconds, could this explain partial binding?.


Comparative effects of R- and S-equol and implication of transactivation functions (AF-1 and AF-2) in estrogen receptor-induced transcriptional activity.

Abstract
Equol, one of the main metabolites of daidzein, is a chiral compound with pleiotropic effects on cellular signaling. This property may induce activation/inhibition of the estrogen receptors (ER) a or b, and therefore, explain the beneficial/deleterious effects of equol on estrogen-dependent diseases. With its asymmetric centre at position C-3, equol can exist in two enantiomeric forms (R- and S-equol). To elucidate the yet unclear mechanisms of ER activation/inhibition by equol, we performed a comprehensive analysis of ERa and ERb transactivation by racemic equol, as well as by enantiomerically pure forms. Racemic equol was prepared by catalytic hydrogenation from daidzein and separated into enantiomers by chiral HPLC. The configuration assignment was performed by optical rotatory power measurements. The ER-induced transactivation by R- and S-equol (0.1-10 µM) and 17b-estradiol (E2, 10 nM) was studied using transient transfections of ERα and ERβ in CHO, HepG2 and HeLa cell lines. R- and S-equol induce ER transactivation in an opposite fashion according to the cellular context. R-equol and S-equol are more potent in inducing ERα in an AF-2 and AF-1 permissive cell line, respectively. Involvement of ERα transactivation functions (AF-1 and AF-2) in these effects has been examined. Both AF-1 and AF-2 are involved in racemic equol, R-equol and S-equol induced ERα transcriptional activity. These results could be of interest to find a specific ligand modulating ER transactivation and could contribute to explaining the diversity of equol actions in vivo.