Pubmed-entry ::= {
  pmid 22326263,
  medent {
    em std {
      year 2012,
      month 3,
      day 19
    },
    cit {
      title {
        name "Recombinant Nox4 cytosolic domain produced by a cell or
 cell-free base systems exhibits constitutive diaphorase activity."
      },
      authors {
        names ml {
          "Nguyen MV",
          "Zhang L",
          "Lhomme S",
          "Mouz N",
          "Lenormand JL",
          "Lardy B",
          "Morel F"
        },
        affil str "GREPI AGIM FRE CNRS-UJF, Universite Joseph Fourier,
 Grenoble, France. mvchuong@yahoo.fr"
      },
      from journal {
        title {
          iso-jta "Biochem. Biophys. Res. Commun.",
          ml-jta "Biochem Biophys Res Commun",
          issn "1090-2104",
          name "Biochemical and biophysical research communications"
        },
        imp {
          date std {
            year 2012,
            month 3,
            day 16
          },
          volume "419",
          issue "3",
          pages "453-458",
          language "eng",
          pubstatus ppublish,
          history {
            {
              pubstatus received,
              date std {
                year 2012,
                month 1,
                day 13
              }
            },
            {
              pubstatus accepted,
              date std {
                year 2012,
                month 1,
                day 27
              }
            },
            {
              pubstatus aheadofprint,
              date std {
                year 2012,
                month 2,
                day 3
              }
            },
            {
              pubstatus other,
              date std {
                year 2012,
                month 2,
                day 14,
                hour 6,
                minute 0
              }
            },
            {
              pubstatus pubmed,
              date std {
                year 2012,
                month 2,
                day 14,
                hour 6,
                minute 0
              }
            },
            {
              pubstatus medline,
              date std {
                year 2012,
                month 5,
                day 9,
                hour 6,
                minute 0
              }
            }
          }
        }
      },
      ids {
        pii "S0006-291X(12)00190-8",
        doi "10.1016/j.bbrc.2012.01.136",
        pubmed 22326263
      }
    },
    abstract "The membrane protein NADPH (nicotinamide adenine dinucleotide
 phosphate) oxidase Nox4 constitutively generates reactive oxygen species
 differing from other NADPH oxidases activity, particularly in Nox2 which
 needs a stimulus to be active. Although the precise mechanism of production
 of reactive oxygen species by Nox2 is well characterized, the electronic
 transfer throughout Nox4 remains unclear. Our study aims to investigate the
 initial electronic transfer step (diaphorase activity) of the cytosolic tail
 of Nox4. For this purpose, we developed two different approaches to produce
 soluble and active truncated Nox4 proteins. We synthesized soluble
 recombinant proteins either by in vitro translation or by bacteria induction.
 While proteins obtained by bacteria induction demonstrate an activity of 4.4
 +/- 1.7 nmol/min/nmol when measured against iodonitro tetrazolium chloride
 and 20.5 +/- 2.8 nmol/min/nmol with cytochrome c, the soluble proteins
 produced by cell-free expression system exhibit a diaphorase activity with a
 turn-over of 26 +/- 2.6 nmol/min/nmol when measured against iodonitro
 tetrazolium chloride and 48 +/- 20.2 nmol/min/nmol with cytochrome c.
 Furthermore, the activity of the soluble proteins is constitutive and does
 not need any stimulus. We also show that the cytosolic tail of the isoform
 Nox4B lacking the first NADPH binding site is unable to demonstrate any
 diaphorase activity pointing out the importance of this domain.",
    mesh {
      {
        term "Cell-Free System"
      },
      {
        term "Cytosol",
        qual {
          {
            subh "enzymology"
          }
        }
      },
      {
        term "Escherichia coli",
        qual {
          {
            subh "enzymology"
          },
          {
            subh "genetics"
          }
        }
      },
      {
        term "HEK293 Cells"
      },
      {
        term "Humans"
      },
      {
        term "NADH Dehydrogenase",
        qual {
          {
            mp TRUE,
            subh "chemistry"
          },
          {
            subh "genetics"
          }
        }
      },
      {
        term "NADPH Oxidase",
        qual {
          {
            mp TRUE,
            subh "chemistry"
          },
          {
            subh "genetics"
          }
        }
      },
      {
        term "Protein Structure, Tertiary"
      },
      {
        term "Recombinant Proteins",
        qual {
          {
            subh "chemistry"
          },
          {
            subh "genetics"
          }
        }
      }
    },
    substance {
      {
        type nameonly,
        name "Recombinant Proteins"
      },
      {
        type ec,
        cit "1.6.3.-",
        name "NOX4 protein, human"
      },
      {
        type ec,
        cit "1.6.3.1",
        name "NADPH Oxidase"
      },
      {
        type ec,
        cit "1.6.99.3",
        name "NADH Dehydrogenase"
      }
    },
    pmid 22326263,
    pub-type {
      "Journal Article",
      "Research Support, Non-U.S. Gov't"
    },
    status medline
  }
}

Other elisa kits Products