<?xml version='1.0' encoding='utf-8'?>
<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:contributor>J. Mark Shrimpton</dc:contributor>
  <dc:contributor>S. D. McCormick</dc:contributor>
  <dc:contributor>Bjorn Thrandur Bjornsson</dc:contributor>
  <dc:creator>Petra Persson</dc:creator>
  <dc:date>2000</dc:date>
  <dc:description>&lt;p&gt;&lt;span&gt;High-affinity, low-capacity estradiol-17β (E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;) binding is present in rainbow trout scale. The&amp;nbsp;&lt;/span&gt;&lt;i&gt;K&lt;/i&gt;&lt;sub&gt;d&lt;/sub&gt;&lt;span&gt;&amp;nbsp;and&amp;nbsp;&lt;/span&gt;&lt;i&gt;B&lt;/i&gt;&lt;sub&gt;max&lt;/sub&gt;&lt;span&gt;&amp;nbsp;of the scale E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;binding are similar to those of the liver E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;receptor (&lt;/span&gt;&lt;i&gt;K&lt;/i&gt;&lt;sub&gt;d&lt;/sub&gt;&lt;span&gt;&amp;nbsp;is 1.6 ± 0.1 and 1.4 ± 0.1 nM, and&amp;nbsp;&lt;/span&gt;&lt;i&gt;B&lt;/i&gt;&lt;sub&gt;max&lt;/sub&gt;&lt;span&gt;&amp;nbsp;is 9.1 ± 1.2 and 23.1 ± 2.2 fmol × mg protein&lt;/span&gt;&lt;sup&gt;-1&lt;/sup&gt;&lt;span&gt;, for scale and liver, respectively), but different from those of the high-affinity, low-capacity E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;binding in plasma (&lt;/span&gt;&lt;i&gt;K&lt;/i&gt;&lt;sub&gt;d&lt;/sub&gt;&lt;span&gt;&amp;nbsp;is 4.0 ± 0.4 nM and&amp;nbsp;&lt;/span&gt;&lt;i&gt;B&lt;/i&gt;&lt;sub&gt;max&lt;/sub&gt;&lt;span&gt;&amp;nbsp;is 625.4 ± 63.1 fmol × mg protein&lt;/span&gt;&lt;sup&gt;−1&lt;/sup&gt;&lt;span&gt;). The E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;binding in scale was displaced by testosterone, but not by diethylstilbestrol. Hence, the ligand binding specificity is different from that of the previously characterized liver E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;receptor, where E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;is displaced by diethylstilbestrol, but not by testosterone. The putative scale E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;receptor thus appears to bind both E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;and testosterone, and it is proposed that the increased scale resorption observed during sexual maturation in both sexes of several salmonid species may be mediated by this receptor. No high-affinity, low-capacity E&lt;/span&gt;&lt;sub&gt;2&lt;/sub&gt;&lt;span&gt;&amp;nbsp;binding could be detected in rainbow trout gill or skin.&lt;/span&gt;&lt;/p&gt;</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>10.1006/gcen.2000.7536</dc:identifier>
  <dc:language>en</dc:language>
  <dc:publisher>Elsevier</dc:publisher>
  <dc:title>The presence of high-affinity, low-capacity estradiol-17β binding in rainbow trout scale indicates a possible endocrine route for the regulation of scale resorption</dc:title>
  <dc:type>article</dc:type>
</oai_dc:dc>