A small computer system for the routine analysis of enzyme kinetic mechanisms
β Scribed by David J. Bates; Carl Frieden
- Publisher
- Elsevier Science
- Year
- 1973
- Tongue
- English
- Weight
- 832 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0010-4809
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β¦ Synopsis
A small computer system was developed to aid in the analysis of full-time course enzyme kinetic or related data through rapid simulation and visual curve fitting. The system is designed to run on a PDP-12/40 computer. It has the capabilities of acquiring data directly, of accepting enzymatic mechanisms in a standard chemical format, and of displaying or plotting the simulated results. Simulation is rapid enough to allow direct user interaction. Examples of how the system may be applied to various common enzymatic mechanisms are given and the general limitations are discussed.
π SIMILAR VOLUMES
We have developed a package program for the estimation of Michaelis-Menten parameters for enzymes that conform to different kinetic mechanisms. Data from different experimental schemes can be fitted with appropriate weighting factors to any of 6 mathematical models, corresponding to 5 kinetic mechan
One-minimum U-shaped temperature profiles of the dissociation constant (K(m)) have been observed experimentally with a variety of enzyme-substrate (E-S) systems. The increase of E-S affinity with falling temperature ("positive thermal modulation of affinity"), which opposes the cold-induced reductio