Kurganov B I, Dorozhko A I, Kagan Z S, Iakovlev V A
Mol Biol (Mosk). 1975 Jul-Aug;9(4):533-42.
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).
对于2p⇌P（P为能够可逆解离形成两个相同半体p的酶寡聚体）和M⇌M₂⇌M₂⇌……（M为具有两个与活性位点重叠的缔合位点的单体）类型的缓慢平衡的缔合-解离酶系统，分析了产物积累与时间（t）的关系曲线形状。假设寡聚体形式之间的平衡速率与总的酶促反应速率相当，并且底物-寡聚体复合物与游离组分处于快速平衡。结果表明，缓慢平衡的缔合-解离酶系统动力学行为的特征是，τ值取决于酶浓度（τ是产物浓度与时间曲线在t趋于无穷大时线性渐近线在t轴上的截距）。
