Biomedical Engineering Reference
In-Depth Information
8000
5000
4000
6000
3000
4000
2000
2000
1000
0
0
0
100
200
300
400
500
0
100
200
300
400
500
A
B
Time (s)
Time (s)
3000
2500
2000
1500
1000
500
0
0
100
200
300
400
C
Time (s)
Figure 8.6
Binding and dissociation of different concentrations (in
M) of oxazaborolidine derivative
m
(BNO1)
þ
2
M sucrose in solution to fructosyltransferase (FTF) immobilized on a SPR sensor chip
surface (
Jabbour et al., 2007
): (a) 0 (b) 60 (c) 600.
m
2007
). A single-fractal analysis is adequate to describe the binding and the dissociation kinet-
ics. The values of (a) the binding rate coefficient,
k
, and the fractal dimension,
D
f
, for a
single-fractal analysis, and (b) the dissociation rate coefficient,
k
d
, and the fractal dimension
for the dissociation phase,
D
fd
, for a single-fractal analysis are given in
Tables 8.4
and
8.5
.
In this case, the affinity,
K
(
¼
k
/
k
d
), value is 19.1.
Figure 8.6b
shows the binding and dissociation of 60
m
M oxazaborolidine derivative,
BNO1
2 mM sucrose in solution to FTF immobilized on a SPR sensor chip surface
(
Jabbour et al., 2007
). A single-fractal analysis is adequate to describe the binding and the
dissociation kinetics. The values of (a) the binding rate coefficient,
k
, and the fractal dimen-
sion,
D
f
, for a single-fractal analysis, and (b) the dissociation rate coefficient,
k
d
, and the
fractal dimension for the dissociation phase,
D
fd
, for a single-fractal analysis are given in
Tables 8.4
and
8.5
. In this case, the affinity,
K
(
þ
¼
k
/
k
d
), value is 11.82.
Figure 8.6c
shows the binding and dissociation of 600
m
M oxazaborolidine derivative,
BNO1
þ
2 mM sucrose in solution to FTF immobilized on a SPR sensor chip surface
