Loading…
Analysis of the substrate inhibition of complete and partial types
A simple graphical method was described for determining the kinetic parameters of substrate inhibition of complete and partial types. The method consists of plotting experimental data as v / V m a x - v versus the reciprocals of the substrate concentrations, where V max represents the maximal veloci...
Saved in:
| Published in: | SpringerPlus 2015-06, Vol.4 (1), p.292-292, Article 292 |
|---|---|
| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | A simple graphical method was described for determining the kinetic parameters of substrate inhibition of complete and partial types. The method consists of plotting experimental data as
v
/
V
m
a
x
-
v
versus the reciprocals of the substrate concentrations, where
V
max
represents the maximal velocity. The reaction rate constant of enzyme–substrate–inhibitor complex
(
k
′
/
k
)
can be calculated from the ordinate intercept of the linear relationship between
v
/
V
m
a
x
-
v
and the reciprocal of the substrate concentrations at the higher and inhibitory concentrations of the substrate: partial type
(
k
′
/
k
<
1
)
of the substrate inhibition gives straight lines intersecting with the ordinate at
(
k
′
/
k
)
/
(
1
-
k
′
/
k
)
, whereas complete substrate inhibition
(
k
′
=
0
)
yields straight lines converging on the origin. The
K
i
′
value also can be calculated from the slope by using the
k
′
/
k
value determined. Validity of the method was confirmed by analyzing the substrate inhibition of phosphofructokinase II from
E. coli
. The present method provides a simple way for determining kinetic parameters of the substrate inhibition irrespective of complete and partial types. |
|---|---|
| ISSN: | 2193-1801 2193-1801 |
| DOI: | 10.1186/s40064-015-1082-8 |