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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: 190000" data-attributes="member: 13851"><p><strong><span style="color: rgb(184, 49, 47)">Figure 2: (Figure 2A)</span> HSA crystal structure showing the fatty acid-binding sites which have been resolved in the crystal structure. <span style="color: rgb(184, 49, 47)">Figure 2B. </span><span style="color: rgb(0, 0, 0)">Panel A: 9</span> resonances observed from 13C-OA binding to HSA <span style="color: rgb(184, 49, 47)">(2 mM OA, 0.5 mM HSA)</span> bound sites. Panels B, C, D show a decrease in NMR signal from binding pockets corresponding to peaks A, E, and F as the OA is displaced by increasing testosterone concentrations. Red resonances in panels B, C, and D are from sites that are occupied by OA in the presence of testosterone. <span style="color: rgb(184, 49, 47)">Panel A </span>shows the spectra obtained from 4:1 ratio of OA: HSA in absence of testosterone; <span style="color: rgb(184, 49, 47)">Panel B:</span> in presence of 0.5 molar equivalents of testosterone, <span style="color: rgb(184, 49, 47)">Panel C:</span> upon addition of 1 molar equivalent of testosterone; and <span style="color: rgb(184, 49, 47)">Panel D:</span> in presence of 2 molar equivalents of testosterone. <span style="color: rgb(184, 49, 47)">Panel E </span>shows the four spectra analyzed using CCPNMR software to determine the peak intensity at corresponding concentrations of testosterone. </strong></p><p>[ATTACH=full]11379[/ATTACH]</p></blockquote><p></p>
[QUOTE="madman, post: 190000, member: 13851"] [B][COLOR=rgb(184, 49, 47)]Figure 2: (Figure 2A)[/COLOR] HSA crystal structure showing the fatty acid-binding sites which have been resolved in the crystal structure. [COLOR=rgb(184, 49, 47)]Figure 2B. [/COLOR][COLOR=rgb(0, 0, 0)]Panel A: 9[/COLOR] resonances observed from 13C-OA binding to HSA [COLOR=rgb(184, 49, 47)](2 mM OA, 0.5 mM HSA)[/COLOR] bound sites. Panels B, C, D show a decrease in NMR signal from binding pockets corresponding to peaks A, E, and F as the OA is displaced by increasing testosterone concentrations. Red resonances in panels B, C, and D are from sites that are occupied by OA in the presence of testosterone. [COLOR=rgb(184, 49, 47)]Panel A [/COLOR]shows the spectra obtained from 4:1 ratio of OA: HSA in absence of testosterone; [COLOR=rgb(184, 49, 47)]Panel B:[/COLOR] in presence of 0.5 molar equivalents of testosterone, [COLOR=rgb(184, 49, 47)]Panel C:[/COLOR] upon addition of 1 molar equivalent of testosterone; and [COLOR=rgb(184, 49, 47)]Panel D:[/COLOR] in presence of 2 molar equivalents of testosterone. [COLOR=rgb(184, 49, 47)]Panel E [/COLOR]shows the four spectra analyzed using CCPNMR software to determine the peak intensity at corresponding concentrations of testosterone. [/B] [ATTACH type="full"]11379[/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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