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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone and Men's Health Articles
Allosterically coupled multi-site binding of T to human serum albumin
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<blockquote data-quote="madman" data-source="post: 190002" data-attributes="member: 13851"><p><strong>Figure 4: <span style="color: rgb(184, 49, 47)">The apparent dissociation constant </span><span style="color: rgb(0, 0, 0)">(Kd)</span><span style="color: rgb(184, 49, 47)"> at 37°C changes as a function of testosterone concentration. </span>The Kd was obtained by using the law of mass action and the measured testosterone concentrations from equilibrium dialysis and mass spectrometry for four different concentrations of <span style="color: rgb(147, 101, 184)">HSA:</span> 450 µM <span style="color: rgb(184, 49, 47)">(Red</span> <span style="color: rgb(184, 49, 47)">circles)</span>, 600 µM <span style="color: rgb(243, 121, 52)">(orange squares)</span>, 750 µM <span style="color: rgb(26, 188, 156)">(green triangles)</span>, and 875 µM <span style="color: rgb(41, 105, 176)">(blue diamonds)</span>. The apparent Kd depends on the ratio of <span style="color: rgb(147, 101, 184)">HSA </span>to testosterone, which is suggestive of allostery and interaction between the binding sites. If there were one binding site for testosterone on <span style="color: rgb(147, 101, 184)">HSA</span>, then the Kd should remain unchanged at a given temperature, but these data show that apparent Kd values for testosterone binding to <span style="color: rgb(147, 101, 184)">HSA</span> changes with their relative concentrations </strong></p><p>[ATTACH=full]11381[/ATTACH]</p></blockquote><p></p>
[QUOTE="madman, post: 190002, member: 13851"] [B]Figure 4: [COLOR=rgb(184, 49, 47)]The apparent dissociation constant [/COLOR][COLOR=rgb(0, 0, 0)](Kd)[/COLOR][COLOR=rgb(184, 49, 47)] at 37°C changes as a function of testosterone concentration. [/COLOR]The Kd was obtained by using the law of mass action and the measured testosterone concentrations from equilibrium dialysis and mass spectrometry for four different concentrations of [COLOR=rgb(147, 101, 184)]HSA:[/COLOR] 450 µM [COLOR=rgb(184, 49, 47)](Red[/COLOR] [COLOR=rgb(184, 49, 47)]circles)[/COLOR], 600 µM [COLOR=rgb(243, 121, 52)](orange squares)[/COLOR], 750 µM [COLOR=rgb(26, 188, 156)](green triangles)[/COLOR], and 875 µM [COLOR=rgb(41, 105, 176)](blue diamonds)[/COLOR]. The apparent Kd depends on the ratio of [COLOR=rgb(147, 101, 184)]HSA [/COLOR]to testosterone, which is suggestive of allostery and interaction between the binding sites. If there were one binding site for testosterone on [COLOR=rgb(147, 101, 184)]HSA[/COLOR], then the Kd should remain unchanged at a given temperature, but these data show that apparent Kd values for testosterone binding to [COLOR=rgb(147, 101, 184)]HSA[/COLOR] changes with their relative concentrations [/B] [ATTACH type="full"]11381[/ATTACH] [/QUOTE]
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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone and Men's Health Articles
Allosterically coupled multi-site binding of T to human serum albumin
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