title: Kinetic analysis of a general model of activation of aspartic proteinase zymogens involving a reversible inhibitor. II. Contribution of the uni- and bimolecular activation routes.
abstract: From the kinetic study carried out in part I of this series (preceding article) an analysis quantifying the relative contribution to the global process of the uni- and bimolecular routes has been carried out. This analysis suggests a way to predict the time course of the relative contribution as well as the effect on this relative weight of the initial zymogen, inhibitor and activating enzyme concentrations.
authors.affiliation: Departamento de Química-Física, Escuela Politécnica Superior de Albacete, Universidad de Castilla-La Mancha, Albacete, Spain.
authors.forename: A
authors.initials: A
authors.lastname: Muñoz-López
authors.forename: A
authors.initials: A
authors.lastname: Sotos-Lomas
authors.forename: E
authors.initials: E
authors.lastname: Arribas
authors.forename: J
authors.initials: J
authors.lastname: Escribano
authors.forename: J
authors.initials: J
authors.lastname: Masia-Perez
authors.forename: J L
authors.initials: JL
authors.lastname: Muñoz-Muñoz
authors.forename: R
authors.initials: R
authors.lastname: Varon
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D002384:Catalysis; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000737:chemistry*; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical
chemical_list: D004791:Enzyme Inhibitors; D004792:Enzyme Precursors; D016282:Aspartic Acid Endopeptidases