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<record>
<TEI>
<teiHeader>
<fileDesc>
<titleStmt>
<title xml:lang="en">Phytotropins</title>
<author>
<name sortKey="Katekar, Gerard F" sort="Katekar, Gerard F" uniqKey="Katekar G" first="Gerard F." last="Katekar">Gerard F. Katekar</name>
</author>
<author>
<name sortKey="Nave, Jean Francois" sort="Nave, Jean Francois" uniqKey="Nave J" first="Jean-François" last="Navé">Jean-François Navé</name>
</author>
<author>
<name sortKey="Geissler, Art E" sort="Geissler, Art E" uniqKey="Geissler A" first="Art E." last="Geissler">Art E. Geissler</name>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">PMC</idno>
<idno type="pmid">16662126</idno>
<idno type="pmc">426121</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC426121</idno>
<idno type="RBID">PMC:426121</idno>
<date when="1981">1981</date>
<idno type="wicri:Area/Pmc/Corpus">001063</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001063</idno>
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<sourceDesc>
<biblStruct>
<analytic>
<title xml:lang="en" level="a" type="main">Phytotropins</title>
<author>
<name sortKey="Katekar, Gerard F" sort="Katekar, Gerard F" uniqKey="Katekar G" first="Gerard F." last="Katekar">Gerard F. Katekar</name>
</author>
<author>
<name sortKey="Nave, Jean Francois" sort="Nave, Jean Francois" uniqKey="Nave J" first="Jean-François" last="Navé">Jean-François Navé</name>
</author>
<author>
<name sortKey="Geissler, Art E" sort="Geissler, Art E" uniqKey="Geissler A" first="Art E." last="Geissler">Art E. Geissler</name>
</author>
</analytic>
<series>
<title level="j">Plant Physiology</title>
<idno type="ISSN">0032-0889</idno>
<idno type="eISSN">1532-2548</idno>
<imprint>
<date when="1981">1981</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass></textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">
<p>Certain members of the phytotropin class of auxin transport inhibitors are shown to bind with high affinity to the known naphthylphthalamic acid binding sites in maize (
<italic>Zea mays</italic>
) coleoptiles. The binding site is, thus, a phytotropin binding site. In general, the degree of binding correlates with the phytotropin structure activity rules and with physiological activities of model compounds. It is argued that the binding site may be a receptor, and it also may be the receptor involved in the control of the auxin transport process. The possibility is raised that the binding sites may be intrinsic receptors for endoanalog(s) of the phytotropins.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article">
<pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">Plant Physiol</journal-id>
<journal-title>Plant Physiology</journal-title>
<issn pub-type="ppub">0032-0889</issn>
<issn pub-type="epub">1532-2548</issn>
</journal-meta>
<article-meta>
<article-id pub-id-type="pmid">16662126</article-id>
<article-id pub-id-type="pmc">426121</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Articles</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Phytotropins</article-title>
<subtitle>III. NAPHTHYLPHTHALAMIC ACID BINDING SITES ON MAIZE COLEOPTILE MEMBRANES AS POSSIBLE RECEPTOR SITES FOR PHYTOTROPIN ACTION</subtitle>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Katekar</surname>
<given-names>Gerard F.</given-names>
</name>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Navé</surname>
<given-names>Jean-François</given-names>
</name>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Geissler</surname>
<given-names>Art E.</given-names>
</name>
</contrib>
</contrib-group>
<aff id="af1">Commonwealth Scientific and Industrial Research Organisation, Division of Plant Industry, Canberra 2601, Australia</aff>
<aff id="af2">Laboratoire de Biochimie Végétale, E. R. A. No. 487, du C. N. R. S., Institut de Botanique, Université Louis Pasteur, 67083 Strasbourg, France</aff>
<pub-date pub-type="ppub">
<month>12</month>
<year>1981</year>
</pub-date>
<volume>68</volume>
<issue>6</issue>
<fpage>1460</fpage>
<lpage>1464</lpage>
<abstract>
<p>Certain members of the phytotropin class of auxin transport inhibitors are shown to bind with high affinity to the known naphthylphthalamic acid binding sites in maize (
<italic>Zea mays</italic>
) coleoptiles. The binding site is, thus, a phytotropin binding site. In general, the degree of binding correlates with the phytotropin structure activity rules and with physiological activities of model compounds. It is argued that the binding site may be a receptor, and it also may be the receptor involved in the control of the auxin transport process. The possibility is raised that the binding sites may be intrinsic receptors for endoanalog(s) of the phytotropins.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>

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