Formation and characterization of glutamate dehydrogenase monolayers on silicon supports (Articolo in rivista)

Type
Label
  • Formation and characterization of glutamate dehydrogenase monolayers on silicon supports (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bios.2004.10.012 (literal)
Alternative label
  • Laura Blasi ; Luigia Longo ; Piero Pompa ; Liberato Manna ; Giuseppe Ciccarella ; Giuseppe Vasapollo ; Roberto Cingolani ; Rosaria Rinaldi ; Antonia Rizzello ; Raffaele Acierno ; Carlo Storelli (2005)
    Formation and characterization of glutamate dehydrogenase monolayers on silicon supports
    in Biosensors & bioelectronics
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Laura Blasi ; Luigia Longo ; Piero Pompa ; Liberato Manna ; Giuseppe Ciccarella ; Giuseppe Vasapollo ; Roberto Cingolani ; Rosaria Rinaldi ; Antonia Rizzello ; Raffaele Acierno ; Carlo Storelli (literal)
Pagina inizio
  • 30 (literal)
Pagina fine
  • 40 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 21 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Natl Nanotechnol Lab, INFM , Dept Innovat Engn, Univ Lecce, I-73100 Lecce, Italy (Laura Blasi ; Piero Pompa ; Liberato Manna ; Roberto Cingolani ; Rosaria Rinaldi ;) 2. Dept Innovat Engn, Univ Lecce, I-73100 Lecce, Italy (Giuseppe Ciccarella ; Giuseppe Vasapollo ;) 3. Univ Lecce, Dept Biol & Environm Sci & Technol, Lab Gen Physiol, I-73100 Lecce, Italy (Antonia Rizzello ; Raffaele Acierno ; Carlo Storelli) (literal)
Titolo
  • Formation and characterization of glutamate dehydrogenase monolayers on silicon supports (literal)
Abstract
  • In this paper we have tested two different procedures (the \"three-step\" and the \"four-step\" procedures) for the covalent immobilization of glutamate dehydrogenase (GDH) onto silicon supports. Atomic force microscopy (AFM), Fourier-transform infrared spectroscopy (FT-IR), fluorescence spectroscopy and an enzymatic assay were used to probe the structure and activity of the immobilized enzyme. Our results demonstrate that coupling through the \"three-step\" procedure does not significantly affect either the fold pattern or the activity of the enzyme, suggesting that this method could be ideally suited to the development of high quality monolayers for use in enzyme-based planar biosensors. (literal)
Autore CNR

Incoming links:


Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it