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<article article-type="research-article" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:mml="http://www.w3.org/1998/Math/MathML">
    <front>
        <journal-meta>
            <journal-id journal-id-type="publisher-id">TOBIOJ</journal-id>
            <journal-title>The Open Biology Journal</journal-title>
            <abbrev-journal-title abbrev-type="pubmed">Open Bio. J.</abbrev-journal-title>
            <issn pub-type="epub">1874-1967</issn>
            <publisher>
                <publisher-name>Bentham Open</publisher-name>
            </publisher>
        </journal-meta>
        <article-meta>
            <article-id pub-id-type="publisher-id">TOBIOJ-1-21</article-id>
            <article-id pub-id-type="doi">10.2174/1874196700801010021</article-id>
            <article-categories>
                <subj-group subj-group-type="heading">
                    <subject>Biology</subject>
                </subj-group>
            </article-categories>
            <title-group>
                <article-title>Isolation and Partial Characterization of an Antiviral Proteolytic Fraction from the Venom of <italic>Echis Carinatus Sochureki</italic></article-title>
            </title-group>
            <contrib-group>
                <contrib contrib-type="author" corresp="yes">
                    <name>
                        <surname>Borkow</surname>
                        <given-names>G.</given-names>
                    </name>
                    <xref ref-type="aff" rid="aff1">1</xref>
                    <xref ref-type="corresp" rid="cor1">&#x002A;</xref>
                </contrib>
                <contrib>
                    <name>
                        <surname>Marco</surname>
                        <given-names>D.</given-names>
                    </name>
                    <xref ref-type="aff" rid="aff2">2</xref>
                </contrib>
                <contrib>
                    <name>
                        <surname>Ovadia</surname>
                        <given-names>M.</given-names>
                    </name>
                    <xref ref-type="aff" rid="aff2">2</xref>
                </contrib>
                <aff id="aff1">
                    <label>1</label>Cupron Inc. Hameyasdim 44, Gibton 76910, Israel, and</aff>
                <aff id="aff2">
                    <label>2</label>Department of Zoology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 69978, Israel</aff>
            </contrib-group>
            <author-notes>
                <corresp id="cor1">
                    <label>&#x002A;</label>Address correspondence to this author at the Cupron Inc. Chemtex, P.O. Box No. 23311, Jerusalem 91233, Israel; Tel: 972-8-546-611287; Fax: 972-8-9491254; 
                    E-mail: <email xlink:href="gadi@cupron.com">gadi@cupron.com</email></corresp>
            </author-notes>
            <pub-date pub-type="epub">
                <day>08</day>
                <month>8</month>
                <year>2008</year>
            </pub-date>
            <pub-date pub-type="collection">
                <year>2008</year>
            </pub-date>
            <volume>1</volume>
            <fpage>21</fpage>
            <lpage>26</lpage>
            <history>
                <date date-type="received">
                    <day>06</day>
                    <month>03</month>
                    <year>2008</year>
                </date>
                <date date-type="rev-recd">
                    <day>07</day>
                    <month>05</month>
                    <year>2008</year>
                </date>
                <date date-type="accepted">
                    <day>02</day>
                    <month>06</month>
                    <year>2008</year>
                </date>
            </history>
            <permissions>
                <copyright-statement>&#x00A9; 2008 Borkow <italic>et al.</italic></copyright-statement>
                <copyright-year>2008</copyright-year>
                <copyright-holder>G. Borkow</copyright-holder>
                <license license-type="open-access" xlink:href="https://creativecommons.org/licenses/by/4.0/legalcode">
                    <p>This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (<uri xlink:href="https://creativecommons.org/licenses/by/4.0/legalcode">https://creativecommons.org/licenses/by/4.0/legalcode</uri>). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.</p>
                </license>
            </permissions>
            <abstract>
                <p>The venom of the viper <italic>Echis carinatus sochureki</italic> suppresses the hemolytic activity of Sendai virus on human
erythrocytes, when pre-incubated with the virions prior to their binding to cells. A fraction (C1), with an IC<sub>50</sub> of 1.25
&#x100001;g/ml, was isolated from the venom. Fraction C1 possesses strong azocollase, azocaseinase and gelatinase activity. The
proteolytic and anti-hemolytic potency of C1 depends on the period and temperature of incubation. Its antiviral activity is
inhibited by Sodium-EDTA but not by PMSF. SDS PAGE of Sendai virus incubated with fraction C1 shows disappearance
of several of the virion high molecular weight bands. We suggest that inhibition of the hemolytic activity of the virions is
probably a result of the cleavage of viral surface proteins, such as the hemagglutinin-neuraminidase glycoprotein found on
the virion envelope that mediates the absorption of the virus to cells.</p>
            </abstract>
        </article-meta>
    </front>
</article>
