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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00002464naa a2200313 4500
001oai:DiVA.org:uu-150584
003SwePub
008110401s1996 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1505842 URI
024a https://doi.org/10.1016/0003-2670(96)00136-52 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Larsson, Tedu Uppsala universitet,Fysikalisk-kemiska institutionen4 aut
2451 0a Electron transfer between cellobiose dehydrogenase and graphite electrodes
264 1b Elsevier,c 1996
338 a print2 rdacarrier
520 a Electron transfer between the enzyme cellobiose dehydrogenase (CDH) and a flavin adenine dinucleotide (FAD) containing a catalytic active fragment of CDH (FAD-fragment) and a graphite electrode, respectively, was established. The current response in the presence of the enzyme substrate for graphite electrodes with CDH or the FAD-fragment adsorbed on the freshly polished graphite surface were compared with that of electrodes where CDH or the FAD-fragment were crosslinked in a redox polymer at the electrode surface. The initial slope, dj/d[S](S=0), where j is the current density and [S](S=0) the zero substrate concentration, was taken as a measure of the substrate response. For the electrodes with enzymes adsorbed directly on the surface, dj/d[S](S=0), was a factor of 3 lower than for electrodes prepared with the polymer mixture. The redox polymer based electrodes, with CDH and with FAD-fragment, both showed a high and close to equal substrate response. In contrast the surface adsorbed CDH gave a much higher substrate response than the FAD-fragment.
700a Elmgren, Maja,d 1964-u Uppsala universitet,Fysikalisk-kemiska institutionen,Fysikalisk kemi4 aut0 (Swepub:uu)majaelmg
700a Lindquist, Sten-Ericu Uppsala universitet,Fysikalisk-kemiska institutionen4 aut0 (Swepub:uu)stenlind
700a Tessema, Merid4 aut
700a Gorton, Lo4 aut
700a Henriksson, Gunnaru Uppsala universitet,Biokemi4 aut
710a Uppsala universitetb Fysikalisk-kemiska institutionen4 org
773t Analytica Chimica Actad : Elsevierg 331:3, s. 207-215q 331:3<207-215x 0003-2670x 1873-4324
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-150584
8564 8u https://doi.org/10.1016/0003-2670(96)00136-5

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