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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone Basics & Questions
Switching From Cream to Injectable T (subQ)
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<blockquote data-quote="madman" data-source="post: 150718" data-attributes="member: 13851"><p>[ATTACH=full]7592[/ATTACH]</p><p>Schematic representation of experimental models of testosterone binding to SHBG. <strong>(a) Linear model of testosterone (T) binding to SHBG as conceptualized by Vermeulen <em>et al.</em> (3), Södergard <em>et al.</em>(4), and Mazer (5).</strong> <strong><span style="color: rgb(184, 49, 47)">(b) New model (ZBJ, schematic adaptation) proposed by Zakharov <em>et al.</em> (34) incorporating the dynamics of allosteric regulation in testosterone binding to SHBG.</span></strong> The different shapes represent conformationally distinct states of SHBG in the dynamic repartitioning of free testosterone into bound forms. <strong>Recent evidence derived from<span style="color: rgb(184, 49, 47)"> new biophysical techniques </span>indicates that <span style="color: rgb(184, 49, 47)">the binding of testosterone to SHBG is a dynamic, multistep process.</span> The <span style="color: rgb(44, 130, 201)">binding of one molecule of testosterone</span> to <span style="color: rgb(44, 130, 201)">the first binding site on an SHBG dimer </span>leads to <span style="color: rgb(44, 130, 201)">conformational rearrangement and allostery between the two binding sites</span>, such that <span style="color: rgb(44, 130, 201)">the second testosterone molecule binds to the second binding site</span> <span style="color: rgb(44, 130, 201)">with</span> <span style="color: rgb(251, 160, 38)">a different binding affinity;</span> <span style="color: rgb(44, 130, 201)">there is</span> <span style="color: rgb(44, 130, 201)">readjustment of </span><span style="color: rgb(251, 160, 38)">equilibria </span><span style="color: rgb(44, 130, 201)">between these interconverting microstates</span>. This <span style="color: rgb(184, 49, 47)">multistep, allosteric model</span> provides <span style="color: rgb(184, 49, 47)">validated estimates of free testosterone</span>, which have close correspondence with <span style="color: rgb(184, 49, 47)">values measured using equilibrium dialysis. </span></strong></p><p></p><p></p><p></p><p></p><p></p><p></p><p><strong>[ATTACH=full]7591[/ATTACH]<span style="color: rgb(184, 49, 47)">Fig. 8B</span> depicts a graph demonstrating that<span style="color: rgb(184, 49, 47)"> depletion of FT by varying SHBG concentration</span> is best described <span style="color: rgb(184, 49, 47)">by the new Multi-step Dynamic Binding Model with Complex Allostery.</span> Constant concentration of testosterone (6, 12 , 17 or 32 nM) was incubated with <span style="color: rgb(184, 49, 47)">increasing SHBG concentrations</span>, and <span style="color: rgb(184, 49, 47)">free testosterone concentration in buffer side was plotted against SHBG concentration.</span> The curves are the result of the fit of data to the new Multi-step Dynamic Binding Model with Complex Allostery.</strong></p></blockquote><p></p>
[QUOTE="madman, post: 150718, member: 13851"] [ATTACH=full]7592[/ATTACH] Schematic representation of experimental models of testosterone binding to SHBG. [B](a) Linear model of testosterone (T) binding to SHBG as conceptualized by Vermeulen [I]et al.[/I] (3), Södergard [I]et al.[/I](4), and Mazer (5).[/B] [B][COLOR=rgb(184, 49, 47)](b) New model (ZBJ, schematic adaptation) proposed by Zakharov [I]et al.[/I] (34) incorporating the dynamics of allosteric regulation in testosterone binding to SHBG.[/COLOR][/B][COLOR=rgb(184, 49, 47)] [/COLOR]The different shapes represent conformationally distinct states of SHBG in the dynamic repartitioning of free testosterone into bound forms. [B]Recent evidence derived from[COLOR=rgb(184, 49, 47)] new biophysical techniques [/COLOR]indicates that [COLOR=rgb(184, 49, 47)]the binding of testosterone to SHBG is a dynamic, multistep process.[/COLOR] The [COLOR=rgb(44, 130, 201)]binding of one molecule of testosterone[/COLOR] to [COLOR=rgb(44, 130, 201)]the first binding site on an SHBG dimer [/COLOR]leads to [COLOR=rgb(44, 130, 201)]conformational rearrangement and allostery between the two binding sites[/COLOR], such that [COLOR=rgb(44, 130, 201)]the second testosterone molecule binds to the second binding site[/COLOR] [COLOR=rgb(44, 130, 201)]with[/COLOR] [COLOR=rgb(251, 160, 38)]a different binding affinity;[/COLOR] [COLOR=rgb(44, 130, 201)]there is[/COLOR] [COLOR=rgb(44, 130, 201)]readjustment of [/COLOR][COLOR=rgb(251, 160, 38)]equilibria [/COLOR][COLOR=rgb(44, 130, 201)]between these interconverting microstates[/COLOR]. This [COLOR=rgb(184, 49, 47)]multistep, allosteric model[/COLOR] provides [COLOR=rgb(184, 49, 47)]validated estimates of free testosterone[/COLOR], which have close correspondence with [COLOR=rgb(184, 49, 47)]values measured using equilibrium dialysis. [/COLOR][/B] [B][ATTACH=full]7591[/ATTACH][COLOR=rgb(184, 49, 47)]Fig. 8B[/COLOR] depicts a graph demonstrating that[COLOR=rgb(184, 49, 47)] depletion of FT by varying SHBG concentration[/COLOR] is best described [COLOR=rgb(184, 49, 47)]by the new Multi-step Dynamic Binding Model with Complex Allostery.[/COLOR] Constant concentration of testosterone (6, 12 , 17 or 32 nM) was incubated with [COLOR=rgb(184, 49, 47)]increasing SHBG concentrations[/COLOR], and [COLOR=rgb(184, 49, 47)]free testosterone concentration in buffer side was plotted against SHBG concentration.[/COLOR] The curves are the result of the fit of data to the new Multi-step Dynamic Binding Model with Complex Allostery.[/B] [/QUOTE]
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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone Basics & Questions
Switching From Cream to Injectable T (subQ)
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