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. 2009 Sep 2;97(5):1244–1253. doi: 10.1016/j.bpj.2009.06.030

Figure 3.

Figure 3

To avoid negative concentrations in Eadapt, j0 (Fig. 2a) is represented as an enzymatic zero-order process. (a) Fully expanded Michaelis-Menten mechanism. The rate equations together with rate constants are shown in the Appendix. To obtain robust homeostasis in A, Eset removes active Eadapt into an inactive form Eadapt under zero-order conditions with Aset given by Eq. 3. (b) Same mechanism as in panel a, but formulating the Michaelis-Menten mechanism under steady-state/rapid equilibrium conditions. Rate equations are given in the Appendix. A zip-archive containing MATLAB and Berkeley Madonna versions of the model shown in Fig. 3 A with instructions and annotation available in the Supporting Material.