| Autor: |
H.C. Hemker, G.M. Willems |
| Přispěvatelé: |
Biochemie |
| Jazyk: |
angličtina |
| Předmět: |
|
| Zdroj: |
Febs Letters, 24(3), 293-295. Elsevier |
| ISSN: |
0014-5793 |
| DOI: |
10.1016/0014-5793(72)80375-2 |
| Popis: |
The usual way of estimating the reaction constants of an enzymatic reaction is by graphical analysis of experimental data in a Lineweaver-Burk plot or related graphs [ 11. The validity of this method depends upon the a priori assumption that steady-state conditions prevail. An~ogously pre-steady state kinetics make a priori presumption that we are dealing with a pre-steady state. Both types of approach rely upon the fact that enzymatic reactions develop in two widely different time scales; the pre-steady state in fractions of seconds, and the steady state in minutes or hours. This difference in time scale is the justification of the usual techniques for solution of the differential equations that govern the process as they essentially are finite perturbation methods [ 21 . In the course of an investigation on the reaction kinetics of blood coagulation the need was felt to estimate the parameters in an experimental situation where we did not know in what time domain of the reaction we were operating, nor even if indeed a sufficiently sharp distinction of time domains was feasible. We thus set out to find a method which would enable us to estimate the parameters in an enzymatic reaction without knowing beforehand that it would behave according to the steady state assumptions. We considered the classical reaction scheme |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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