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(= extended X-ray absorption fine structure (EXAFS))
A linearized display of kinetic data of dependence of enzyme activity on substrate concentration; rate is plotted against the ratio of rate to substrate concentration. (see also Lineweaver-Burk plot)
A graphical method for determination of enzyme-inhibitor dissociation constants for non-competitive inhibitors, especially those that bind very tightly. Where I is the total inhibitor concentration, E is the total enzyme concentration and is the ratio of inhibited to non-inhibited rates under the same conditions, I/ is plotted on the ordinate (y-axis) against 1/(I-) on the abscissa (x-axis) to give a straight line that intersects the ordinate at E; its slope is Kd, the dissociation constant. (see also Cornish-Bowden plot; Dixon plot; Hunter and Downs plot) Learn more about restriction enzymes.
A chemical technique to degrade and cleave amino acid residues sequentially from a protein beginning at the N-terminus, and to identify the residues as they are removed. Reaction of the N-terminal residue with phenylisothiocyanate cleaves it from the protein as the phenylthiohydantoin derivative, which may be isolated and identified. (see also thiocyanate degradation)Edman, P. (1950) Acta Chim. Scand. 4, 283-293 Learn more about amino acid chart.
The sequence of enzymic reactions that convert glucose into pyruvic acid; also called aerobic glycolysis. (see also glycolysis)
The metabolism of glucose, e.g. by Pseudomonas fluorescens, via 6-phosphogluconic acid and 2-oxo-3-deoxy-6-phosphogluconic acid to pyruvate and glyceraldehyde 3-phosphate.
An enteric bacterium that inhabits the human intestine; much used for experimentation.
(see eukaryote)
(see eukaryote)
see membrane protein secretase
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