1975
DOI: 10.1021/ac60352a006
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Model for the amperometric enzyme electrode obtained through digital simulation and applied to the immobilized glucose oxidase system

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Cited by 299 publications
(127 citation statements)
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“…The response of the electrode exhibits characteristics of the Michaelis-Menten kinetic mechanism. The apparent Michaelis-Menten constant, Km, of tyrosinase on the tyrosinase, NG-MTP-Au electrode to substrate can be calculated according to the Lineweaver-Burk equation, 9,[17][18][19] …”
Section: Amperometric Resultsmentioning
confidence: 99%
“…The response of the electrode exhibits characteristics of the Michaelis-Menten kinetic mechanism. The apparent Michaelis-Menten constant, Km, of tyrosinase on the tyrosinase, NG-MTP-Au electrode to substrate can be calculated according to the Lineweaver-Burk equation, 9,[17][18][19] …”
Section: Amperometric Resultsmentioning
confidence: 99%
“…The flattening of the calibration curves at higher concentrations is dictated by Michaelis-Menten kinetics. It is possible to see that at lower levels the enzyme reaction approximates the first order kinetics whereas at highest concentrations the reaction order approaches zero and the measured current becomes independent of glucose (enzyme substrate) concentration (Mell & Maloy, 1974) The wide measured concentration range and extremely low limit of detection is the result of nanostructure as mentioned in section 1. The immobilization is made by this manner that www.intechopen.com …”
Section: Measurement Of Glucose Oxidase By Electrochemical Sensor Witmentioning
confidence: 90%
“…The apparent Michaelis-Menten constant, K m, a reflection of enzymatic affinity, can be calculated according to the Lineweaver-Burk equation ([Mell and Maloy, 1975], [Shu and Wilson, 1976] and [Kamin and Wilson, 1980]). …”
Section: Amperometric Detection Of Superoxide Radicalmentioning
confidence: 99%