<?xml version="1.0" encoding="UTF-8"?>
<collection xmlns="http://www.loc.gov/MARC21/slim">
 <record>
  <leader>     caa a22        4500</leader>
  <controlfield tag="001">477110738</controlfield>
  <controlfield tag="003">CHVBK</controlfield>
  <controlfield tag="005">20180405111608.0</controlfield>
  <controlfield tag="007">cr unu---uuuuu</controlfield>
  <controlfield tag="008">170330e19960901xx      s     000 0 eng  </controlfield>
  <datafield tag="024" ind1="7" ind2="0">
   <subfield code="a">10.1007/BF00035055</subfield>
   <subfield code="2">doi</subfield>
  </datafield>
  <datafield tag="035" ind1=" " ind2=" ">
   <subfield code="a">(NATIONALLICENCE)springer-10.1007/BF00035055</subfield>
  </datafield>
  <datafield tag="245" ind1="0" ind2="0">
   <subfield code="a">Comparison of rhizobitoxine-induced inhibition of β-cystathionase from different bradyrhizobia and soybean genotypes</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[K. Xiong, J. Fuhrmann]</subfield>
  </datafield>
  <datafield tag="520" ind1="3" ind2=" ">
   <subfield code="a">The enzyme β-cystathionase catalyzes the conversion of cystathionine to homocysteine in both plants and bacteria. Preparations of this enzyme taken from both Salmonella and spinach (Spinacia oleracea L.) have been shown to be irreversibly inhibited by low concentrations of rhizobitoxine (RT), a chlorosis-inducing phytotoxin produced by some strains of soybean bradyrhizobia. The sensitivities of β-cystathionase from bradyrhizobia and soybean are not well characterized. Therefore, we purified β-cystathionase from selected bradyrhizobia and soybean genotypes that have been shown to exhibit differences in RT production and apparent RT sensitivities, respectively. Enzyme purified from E. coli strain DH52 was used for comparison. The enzymes differed in their physiological properties and RT sensitivities. Overall, the β-cystathionase enzymes purified from bradyrhizobia were more sensitive to RT than were those from the soybean cultivars. Kinetic studies showed that the nature of the RT-induced inhibition also differed between the two sources. The enzymes from bradyrhizobia exhibited inhibition that was [RT]-dependent, whereas the enzymes from soybean showed a time-dependent inhibition. These contrasting characteristics may in part reflect differences in active site accessibility, amino acid components, and associated RT diffusion rates. However, in all cases the inhibition caused by RT showed a typical substrate-competitive inhibition pattern.</subfield>
  </datafield>
  <datafield tag="540" ind1=" " ind2=" ">
   <subfield code="a">Kluwer Academic Publishers, 1996</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">β-cystathionase</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">rhizobitoxine</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">secondary RT inhibition constant</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">RT : rhizobitoxine</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">PLP : pyridoxal phosphate</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">DTT : dithioerythritol</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">PMSF : phenylmethylsulfonyl fluoride</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">HTP : hydroxyapatite</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Xiong</subfield>
   <subfield code="D">K.</subfield>
   <subfield code="u">Delaware Agricultural Experiment Station, Department of Plant and Soil Sciences, College of Agricultural Sciences, University of Delaware, 19717-1303, Newark, DE, USA</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Fuhrmann</subfield>
   <subfield code="D">J.</subfield>
   <subfield code="u">Delaware Agricultural Experiment Station, Department of Plant and Soil Sciences, College of Agricultural Sciences, University of Delaware, 19717-1303, Newark, DE, USA</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="773" ind1="0" ind2=" ">
   <subfield code="t">Plant and Soil</subfield>
   <subfield code="d">Kluwer Academic Publishers; http://www.wkap.nl</subfield>
   <subfield code="g">186/1(1996-09-01), 53-61</subfield>
   <subfield code="x">0032-079X</subfield>
   <subfield code="q">186:1&lt;53</subfield>
   <subfield code="1">1996</subfield>
   <subfield code="2">186</subfield>
   <subfield code="o">11104</subfield>
  </datafield>
  <datafield tag="856" ind1="4" ind2="0">
   <subfield code="u">https://doi.org/10.1007/BF00035055</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/BF00035055</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">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Xiong</subfield>
   <subfield code="D">K.</subfield>
   <subfield code="u">Delaware Agricultural Experiment Station, Department of Plant and Soil Sciences, College of Agricultural Sciences, University of Delaware, 19717-1303, Newark, DE, USA</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Fuhrmann</subfield>
   <subfield code="D">J.</subfield>
   <subfield code="u">Delaware Agricultural Experiment Station, Department of Plant and Soil Sciences, College of Agricultural Sciences, University of Delaware, 19717-1303, Newark, DE, USA</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">Plant and Soil</subfield>
   <subfield code="d">Kluwer Academic Publishers; http://www.wkap.nl/</subfield>
   <subfield code="g">186/1(1996-09-01), 53-61</subfield>
   <subfield code="x">0032-079X</subfield>
   <subfield code="q">186:1&lt;53</subfield>
   <subfield code="1">1996</subfield>
   <subfield code="2">186</subfield>
   <subfield code="o">11104</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>
