Biomedical Engineering Reference
In-Depth Information
reaction is reversible), we can express the interaction as.
IGF-I + IGFBP k +1
k 1
IGF/IGFBP
(11.33)
where k +1 is the rate constant for the association reaction (binding) and k 1
is the rate constant for the dissociation reaction. Ignoring the possibility of
diffusion and advection of fixed IGFBPs and complexes, the law of mass action
[68] can be used to quantitatively describe the IGF-I and IGFBP interaction
and leads to the following set of differential equations.
dc I
dt
= k +1 c I c b BP
k 1 c I
(11.34a)
dc b BP
dt
k +1 c I c b BP + k 1 c I
=
(11.34b)
Summing equations (11.34a) and (11.43b) it is easily confirmed that when
there is no net production/degradation of binding proteins
dc b BP
dt
+ dc I
dt
= 0
(11.35)
Thus, c b BP ( t )+ c I ( t )= m . The integration constant, m , can be obtained
using the initial condition, and leads to
c b BP ( t )+ c I ( t )= c b BP 0 + c I 0 ,
where c b BP ( t =0)= c b BP 0 , c I ( t =0)= c I 0
(11.36)
Finally, equation (11.36) is substituted into (11.34a) to obtain
= k +1 c b BP 0 + c I 0
c I c I
dc I
dt
k 1 c I
(11.37)
Equation (11.37) provides a relationship linking c I and c I .
11.3.2.2
Model of Solute Transport and Binding in
a Deformable Cartilage
Now that IGF-I is able to bind to IGFBPs on the solid phase, the solute
conservation law derived previously needs to be modified and an additional
expression needs to be introduced for solute conservation on the solid phase.
Specifically the conservation of mass of solute in the free and bound state can
be described by
φ f c I
∂t
c I + φ f v f c I = −s
−φ f D
+ ∇•
(11.38)
1
φ f c I
∂t
−∇• 1
φ f v s c I = s
(11.39)
 
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