Biomedical Engineering Reference
In-Depth Information
The equations that describe this system in Eqs. (8.114) and (8.115) are
q S ¼ K 1
q C 1 K
q S q E
1
q C 1 ¼ K
q S q E K 1
ð
þ K
Þ q C 1
1
2
ð
8
:
116
Þ
q I ¼ K 3 q C 2 K 2 q I q E
q C 2 ¼ K
q I q E K 3
ð
þ K
Þ q C 2
3
4
We eliminate
q E from Eq. (8.116) by using
q E ¼ E
q C 1 q C 2 , giving
0
q S ¼ K
ð
q S þ K 1
Þ q C 1 þ K
q S q C 2 K
E
q S
1
1
1
0
q C 1 ¼ K 1 E 0 q S K 1 q S þ K 1 þ K 2
ð
Þ q C 1 K 1 q S q C 2
ð
8
:
117
Þ
q I ¼ K
ð
q I þ K 3
Þ q C 2 þ K
q I q C 1 K
E
q I
3
3
3
0
q C 2 ¼ K
E
q I K
ð
q I þ K 3
þ K
Þ q C 2 K
q I q C 1
3
0
3
4
3
with nonzero initial conditions of
Þ¼ E 0 :
The quasi-steady-state approximation is found from Eq. (8.117) with
q S ð
0
Þ¼ S 0 ,
q I ð
0
Þ¼ I 0 and
q E ð
0
q C 1 ¼ q C 2 ¼
0,
yielding
0
¼ K 1 E 0 q S K 1 q S þ K 1 þ K 2
ð
Þ q C 1 K 1 q S q C 2
ð
8
:
118
Þ
0
¼ K 3 E 0 q I K 3 q I þ K 3 þ K 4
ð
Þ q C 2 K 3 q I q C 1
Next, we solve for
q C 2 , which gives
q C 2 ¼ K
q I E
ð
q C 1
Þ
3
0
ð
8
:
119
Þ
q I þ K 3
þ K
K
3
4
and then we solve for
q C 1 , giving
E
q S
0
q C 1 ¼
ð
8
:
120
Þ
þ q I
K i M
q S þ K s M
1
K s M ¼ K 1 þ K 2
K i M ¼ K 3 þ K 4
where
and
:
The velocity of the reaction is given by
K 1
K 3
K
E
q S
V
2
0
max
¼
V ¼ K 2 q C 1 ¼
ð
8
:
121
Þ
K s M
q S
þ q I
K i M
þ q I
K i M
q S þ K s M
1
1
þ
1
where
:
Comparing Eq. (8.121) with Eq. (8.47), we see that
V
¼ K
E
max
2
0
V
max does not change with the inclu-
K M in Eq. (8.47) has been replaced by the
sion of an enzyme inhibitor. In this case the term
in Eq. (8.121), which reduces the reaction rate. The left side of Figure 8.27
shows a plot of the reaction rate versus the substrate with increasing quantities of the
þ q I
K i M
term
K s M
1
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