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@ARTICLE{Fischer:46868,
      author       = {Fischer, T. and Beyermann, M. and Koch, K.-W.},
      title        = {{A}pplication of different surface plasmon resonance
                      biosensor chips to monitor the interaction of the
                      {C}a{M}-binding site of nitric oxide synthase {I} and
                      calmodulin},
      journal      = {Biochemical and biophysical research communications},
      volume       = {285},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-46868},
      pages        = {463 - 469},
      year         = {2001},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Surface plasmon resonance biosensors depend on modified
                      gold surfaces to allow immobilization of proteins or
                      peptides for interaction analysis. We investigated sensor
                      chip surfaces that differ in the geometry of the
                      immobilization matrix: two contain a three-dimensional
                      coupling matrix and two have a surface with immobilization
                      sites on a two-dimensional plane. Properties of sensor chips
                      were compared by studying the interaction of calmodulin with
                      a peptide representing the calmodulin-binding site of nitric
                      oxide synthase I. Apparent K(D) values were determined by
                      three different procedures in order to apply tests for
                      self-consistency. At low surface densities (5-8 fmol/mm(2))
                      on three of the four tested surfaces, estimated K(D) values
                      were within one order of magnitude and similar to the value
                      found in solution (K(D) = 1-3 nM). When immobilization
                      densities were increased by one to two orders of magnitude,
                      apparent association rate constants were less distorted on a
                      flat carboxymethylated surface than on dextran-coated sensor
                      chips.},
      keywords     = {Amino Acid Sequence / Animals / Binding Sites / Biosensing
                      Techniques / Calmodulin: chemistry / Calmodulin: metabolism
                      / Kinetics / Molecular Sequence Data / Nitric Oxide
                      Synthase: chemistry / Nitric Oxide Synthase: metabolism /
                      Nitric Oxide Synthase Type I / Peptides: chemistry /
                      Peptides: metabolism / Rats / Surface Plasmon Resonance:
                      methods / Calmodulin (NLM Chemicals) / Peptides (NLM
                      Chemicals) / Nitric Oxide Synthase (NLM Chemicals) / Nitric
                      Oxide Synthase Type I (NLM Chemicals) / Nos1 protein, rat
                      (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB57},
      pnm          = {Zelluläre Signalverarbeitung},
      pid          = {G:(DE-Juel1)FUEK95},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:11444865},
      UT           = {WOS:000170020900046},
      doi          = {10.1006/bbrc.2001.5206},
      url          = {https://juser.fz-juelich.de/record/46868},
}