948 resultados para Frontal disk
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Mode of access: Internet.
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"March 1984."
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Mode of access: Internet.
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Glass, Roman; D: 4 51/64 in.; carved and blown, cameo glass
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"October 1991."
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Includes index.
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Includes index.
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"February 1984."
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Contribution from Production and Marketing Administration.
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Mode of access: Internet.
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see inscriptions and label on portrait from same studio session, na18169
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Mode of access: Internet.
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Rotating disk voltammetry is routinely used to study electrochemically driven enzyme catalysis because of the assumption that the method produces a steady-state system. This assumption is based on the sigmoidal shape of the voltammograms. We have introduced an electrochemical adaptation of the King-Altman method to simulate voltammograms in which the enzyme catalysis, within an immobilized enzyme layer, is steadystate. This method is readily adaptable to any mechanism and provides a readily programmable means of obtaining closed form analytical equations for a steady-state system. The steady-state simulations are compared to fully implicit finite difference (FIFD) simulations carried out without any steady-state assumptions. On the basis of our simulations, we conclude that, under typical experimental conditions, steady-state enzyme catalysis is unlikely to occur within electrode-immobilized enzyme layers and that typically sigmoidal rotating disk voltammograms merely reflect a mass transfer steady state as opposed to a true steady state of enzyme intermediates at each potential.