<?xml version="1.0" encoding="UTF-8"?>
<collection xmlns="http://www.loc.gov/MARC21/slim">
 <record>
  <leader>     caa a22        4500</leader>
  <controlfield tag="001">445342617</controlfield>
  <controlfield tag="003">CHVBK</controlfield>
  <controlfield tag="005">20180317142818.0</controlfield>
  <controlfield tag="007">cr unu---uuuuu</controlfield>
  <controlfield tag="008">170323e20110301xx      s     000 0 eng  </controlfield>
  <datafield tag="024" ind1="7" ind2="0">
   <subfield code="a">10.1007/s00436-010-2108-3</subfield>
   <subfield code="2">doi</subfield>
  </datafield>
  <datafield tag="035" ind1=" " ind2=" ">
   <subfield code="a">(NATIONALLICENCE)springer-10.1007/s00436-010-2108-3</subfield>
  </datafield>
  <datafield tag="100" ind1="1" ind2=" ">
   <subfield code="a">Moczoń</subfield>
   <subfield code="D">Tadeusz</subfield>
   <subfield code="u">W. Stefański Institute of Parasitology, Polish Academy of Sciences, Twarda 51/55, 00-818, Warszawa, Poland</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="245" ind1="1" ind2="2">
   <subfield code="a">A cysteine proteinase in the penetration glands of the cercariae of Cotylurus cornutus (Trematoda, Strigeidae)</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Tadeusz Moczoń]</subfield>
  </datafield>
  <datafield tag="520" ind1="3" ind2=" ">
   <subfield code="a">A cysteine proteinase from the penetration glands of Cotylurus cornutus cercariae was examined with histochemical and biochemical methods. The enzyme hydrolyzed gelatin, azocoll, azocasein, azoalbumin, N-blocked-l-arginine-4-methoxy-2-naphthylamide, and N-blocked-p-nitroanilide, but did not degrade elastin. The metal ion complexane ethylenediamine tetraacetate and the thiol-reducing compound dithioerythritol enhanced the proteinase activity, whereas the thiol-blocking compounds p-hydroxymercuribenzoate and N-ethylmaleimide (NEM) inhibited it. The enzyme was also sensitive to leupeptin but insensitive to soybean trypsin inhibitor. An electrophoretic separation of extract proteins from the cercariae under acidic, non-denaturing conditions and in the presence of 0.1% gelatin in a polyacrylamide gel revealed the presence of two distinct and three weak transparent bands in the gel resulting from a gelatinolytic activity at pH6.8. The distinct bands apparently resulted from the activity of the glandular enzyme and lysosomal cathepsin B, whereas the weak ones presumably indicated these enzymes partially degraded in the course of the preparative procedure. No gelatinolysis occurred following treatment of an extract sample with 0.1mM NEM.</subfield>
  </datafield>
  <datafield tag="540" ind1=" " ind2=" ">
   <subfield code="a">The Author(s), 2010</subfield>
  </datafield>
  <datafield tag="773" ind1="0" ind2=" ">
   <subfield code="t">Parasitology Research</subfield>
   <subfield code="d">Springer-Verlag</subfield>
   <subfield code="g">108/3(2011-03-01), 639-643</subfield>
   <subfield code="x">0932-0113</subfield>
   <subfield code="q">108:3&lt;639</subfield>
   <subfield code="1">2011</subfield>
   <subfield code="2">108</subfield>
   <subfield code="o">436</subfield>
  </datafield>
  <datafield tag="856" ind1="4" ind2="0">
   <subfield code="u">https://doi.org/10.1007/s00436-010-2108-3</subfield>
   <subfield code="q">text/html</subfield>
   <subfield code="z">Onlinezugriff via DOI</subfield>
  </datafield>
  <datafield tag="908" ind1=" " ind2=" ">
   <subfield code="D">1</subfield>
   <subfield code="a">research-article</subfield>
   <subfield code="2">jats</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">856</subfield>
   <subfield code="E">40</subfield>
   <subfield code="u">https://doi.org/10.1007/s00436-010-2108-3</subfield>
   <subfield code="q">text/html</subfield>
   <subfield code="z">Onlinezugriff via DOI</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">100</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Moczoń</subfield>
   <subfield code="D">Tadeusz</subfield>
   <subfield code="u">W. Stefański Institute of Parasitology, Polish Academy of Sciences, Twarda 51/55, 00-818, Warszawa, Poland</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">773</subfield>
   <subfield code="E">0-</subfield>
   <subfield code="t">Parasitology Research</subfield>
   <subfield code="d">Springer-Verlag</subfield>
   <subfield code="g">108/3(2011-03-01), 639-643</subfield>
   <subfield code="x">0932-0113</subfield>
   <subfield code="q">108:3&lt;639</subfield>
   <subfield code="1">2011</subfield>
   <subfield code="2">108</subfield>
   <subfield code="o">436</subfield>
  </datafield>
  <datafield tag="900" ind1=" " ind2="7">
   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="898" ind1=" " ind2=" ">
   <subfield code="a">BK010053</subfield>
   <subfield code="b">XK010053</subfield>
   <subfield code="c">XK010000</subfield>
  </datafield>
  <datafield tag="949" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="F">NATIONALLICENCE</subfield>
   <subfield code="b">NL-springer</subfield>
  </datafield>
 </record>
</collection>
