title: [Kinetic behavior of slowly equilibrating association-dissociation enzyme systems].
abstract: The shape of the plots of product accumulation versus time (t) has been analysed for slowly equilibrating association-dissociation enzyme systems of the types 2p in equilibrium P (P is enzyme oligomer which is able to dissociate reversibly forming two identical halves p) and M in equilibrium M2 in equilibrium M2 in equilibrium... (M is monomer which has two association sites overlapping with active sites). It is assumed that the rate of equilibration between oligomeric forms is comparable with the rate of over-all enzymatic reaction and that substrate-oligomer complexes are in rapid equilibrium with free components. It has been shown that characteristic feature of kinetic behavior of slowly equilibrating association-dissociation enzyme systems is that the value of tau depends on enzyme concentration (tau is the intercept on t-axis for linear asymptota of the curve of product concentration versus time at t leads to infinity).
mesh_terms: D001665:Binding Sites; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D011485:Protein Binding; D013997:Time Factors
chemical_list: D004798:Enzymes
vernacular_title: Osobennosti kineticheskogo povedeniia medlenno dissotsiiruiushchikh i assotsiiruiushchikh fermentnykh sistem