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      <ref-type name="Journal Article">17</ref-type>
      <contributors>
        <authors>
          <author>A. Atta</author>
          <author>Z. Hashim</author>
          <author>S. Zarina</author>
        </authors>
      </contributors>
      <titles>
        <title>LENS PROTEOMICS: EXPLORING ADAPTIVE CONFLICT IN UROMASTYX HARDWICKII LENS PROTEINS</title>
        <secondary-title>Journal of Animal and Plant Sciences</secondary-title>
        <alt-title>JAPS</alt-title>
      </titles>
      <dates><year>2016</year><pub-dates><date>2016/02/01</date></pub-dates></dates>
      <volume>26</volume>
      <number>1</number>
      <pages>261-268</pages>
      <isbn>1018-7081</isbn>
      <electronic-resource-num>NA</electronic-resource-num>
      <abstract>&lt;p&gt;During last decade, proteomics has emerged as a powerful tool for high throughput screening, identification and quantification of proteins from biological samples. In current study, we have employed proteomics technique to explore proteins from eye lenses of&amp;nbsp;&lt;em&gt;Uromastyx hardwickii,&amp;nbsp;&lt;/em&gt;an Indian spiny-tailed lizard. Water soluble and insoluble proteins from&amp;nbsp;&lt;em&gt;Uromastyx hardwickii&lt;/em&gt;&amp;nbsp;lens were separated and characterized by 2-DE (two dimensional electrophoresis). After in-gel digestion, well resolved spots were identified by nano- liquid chromatography-electrospray tandem mass spectrometry (nLC-MS/MS). We have identified &amp;alpha;A-, &amp;beta;A2-, &amp;beta;A4-, &amp;beta;B2- and &amp;beta;B3-crystallins as ubiquitous crystallins and &amp;delta;-, &amp;tau;-crystallins as taxon-specific lens crystallins in water soluble fraction. &amp;alpha;A- and &amp;beta;B3-crystallins were found to be most abundant water soluble proteins in&amp;nbsp;&lt;em&gt;Uromastyx hardwickii&amp;nbsp;&lt;/em&gt;lens. Among non-crystallins (cellular proteins), &amp;beta;-actin was identified. From water insoluble fraction, vimentin, gelsolin, gamma enolase like protein, filensin like protein and ATP synthase subunit B were identified. Our results illustrate advantage of proteomics technology for identification of lens proteins. Furthermore, the study provides distribution patterns of ubiquitous and taxon specific crystallins from&amp;nbsp;&lt;em&gt;Uromastyx hardwickii&lt;/em&gt; that is likely to be useful in understanding evolutionary lineage of this organism.&lt;/p&gt;</abstract>
      <keywords><keyword>Lens proteomics, ubiquitous lens crystallin, taxon specific lens crystallin, Uromastyx hardwickii, water insoluble lens protein</keyword></keywords>
      <publisher>Pakistan Agricultural Scientists Forum</publisher>
      <urls><related-urls><url>https://thejaps.org.pk/AbstractView.aspx?mid=2016-JAPS-33</url></related-urls></urls>
    </record>
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