<?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>Charles O. Knowles</dc:contributor>
  <dc:creator>James W. Hogan</dc:creator>
  <dc:date>1968</dc:date>
  <dc:description>&lt;p&gt;&lt;span&gt;Using a manometric technique an acetylcholinesterase (EC 3.1.1.7, acetylcholine acetyl-hydrolase) was demonstrated in brain tissue from the bluegill,&amp;nbsp;&lt;/span&gt;&lt;i&gt;Lepomis macrochirus&lt;/i&gt;&lt;span&gt;&amp;nbsp;Rafinesque, and the channel catfish,&amp;nbsp;&lt;/span&gt;&lt;i&gt;Ictalurus punctatus&lt;/i&gt;&lt;span&gt;&amp;nbsp;(Walbaum). The activities were 19 and 37&amp;ensp;&amp;mu;moles acetylcholine hydrolyzed/milligram protein per hour for the bluegill and channel catfish enzymes, respectively. The optimum substrate concentration for the hydrolysis of acetylcholine was 10&amp;ensp;m&lt;/span&gt;&lt;span class="smallcaps"&gt;M&lt;/span&gt;&lt;span&gt;for the enzymes from both species. Generally, the catfish acetylcholinesterase was somewhat more susceptible than the bluegill to the inhibitors tested; however, the bluegill enzyme was more susceptible to inhibition by malathion and malaoxon.&lt;/span&gt;&lt;/p&gt;</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>10.1139/f68-059</dc:identifier>
  <dc:language>en</dc:language>
  <dc:publisher>NRC Research Press</dc:publisher>
  <dc:title>Some enzymatic properties of brain Acetylcholinesterase from bluegill and channel catfish</dc:title>
  <dc:type>article</dc:type>
</oai_dc:dc>