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Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action

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Publication:652730
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DOI10.1007/s10910-011-9869-5zbMath1227.92031OpenAlexW2077064617MaRDI QIDQ652730

Volnei Brito de Souza, Jose Ailton Conceicao Bispo, Giovani Brandao Mafra de Carvalho, Carlos Francisco Sampaio Bonafe, João Batista de Almeida e Silva

Publication date: 15 December 2011

Published in: Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1007/s10910-011-9869-5

zbMATH Keywords

optimizationfermentationBriggs-Haldanecellular growthenzyme catalysisMonodperoxidase


Mathematics Subject Classification ID

Classical flows, reactions, etc. in chemistry (92E20) Dynamical systems in biology (37N25) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)


Related Items

Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation, Applying structural transition theory to describe enzyme kinetics in heterogeneous systems



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