Model for Oxygen binding to myoglobin, single site first order binding.

Description

 Binding of a ligand is a function of the affinity of 
the site for the ligand. The disociation constant is ratio of the off-rate, k_1, to 
the on-rate, k1, is Kd = k_1/k1. 
The binding of oxygen (O2) to myoglobin (Mb) is given by the reaction:

                   k1
                  --->
          O2 + Mb <--- MbO2 , where one O2 molecule binds to the site on Mb.
                   k_1

To translate from physiological measurement of the partial pressure of O2 in units of 
mmHg to molar concentration, the solubility of O2 in water for the particular temperature 
has to be used (alphO2). The PO2 at 50% saturation, i.e. 50% of Mb bound to O2, is 
called p50Mb, and is the PO2 at which the molar concentration of O2 equals Kd.
    In this model, the PO2 is raised gradually in order to run it through a 
wide range of concentrations from well below Kd to well above Kd. If the rate
of binding is slow, the binding will not be at equilibrium, and saturation 
will be below the equilibrium level when PO2 is rising fast.
Change the "rateO2" at which the pO2 is raised: at low on-rates (k1) the SMb 
(the myoglobin saturation) will lag behind the curve for instantaneous equilibration, SMbeq.
 SMbeq = 1/(1+ Kd / pO2),  where Kd is the dissociation constant.

Equations

The equations for this model may be viewed by running the JSim model applet and clicking on the Source tab at the bottom left of JSim's Run Time graphical user interface. The equations are written in JSim's Mathematical Modeling Language (MML). See the Introduction to MML and the MML Reference Manual. Additional documentation for MML can be found by using the search option at the Physiome home page.