1984
DOI: 10.1080/00021369.1984.10866431
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Electrocatalysis with a Glucose-Oxidase-immobilized Graphite Electrode

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Cited by 22 publications
(25 citation statements)
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“…7 6- 7 9 Segments of the polyelectrolyte were designed to either hydrogenbond to the enzyme protein or to electrostatically interact with oppositely charged domains of the enzyme protein. …”
Section: Principles Of Wire Designmentioning
confidence: 99%
“…7 6- 7 9 Segments of the polyelectrolyte were designed to either hydrogenbond to the enzyme protein or to electrostatically interact with oppositely charged domains of the enzyme protein. …”
Section: Principles Of Wire Designmentioning
confidence: 99%
“…5 The dimer contains two disulfide bonds and two free sulfhydryl groups. Using hydroquinone (HQ)/1,4-benzoquinone (BQ) redox couple as an electron mediator, 6 the inactivation of GOD can be followed by the time-dependent decrease in the HQ/BQ-mediated bioelectrocatalytic current. The kinetic measurements were performed in phosphate buffer in the absence and presence of a denaturant, guanidine hydrochloride (GuHCl).…”
Section: Introductionmentioning
confidence: 99%
“…19 Under this condition, the GOx enzymatic reactions and the GOx enzymatic reaction promoted by εPL have been described by the simple Michaelis-Menten equation. 8,20,21 Thus, the rate of the GOx enzymatic reaction promoted by ST, vE, may also be given as…”
Section: Promotion Effect Of Stmentioning
confidence: 99%