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Enzyme Kinetics: Dissociation Constant, Law of Dilution, Allosteric Regulation, Cooperative Binding, Michaelis-menten Kinetics, Abt
Paperback. Books LLC 2010-05-05.
ISBN 9781155619446
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Buy from Amazon.co.uk
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Publisher description
Purchase includes free access to book updates online and a free trial membership in the publisher's book club where you can select from more than a million books without charge. Chapters: Dissociation Constant, Law of Dilution, Allosteric Regulation, Cooperative Binding, Michaelis-menten Kinetics, Abts, Competitive Inhibition, Goldbeter-Koshland Kinetics, Hill Equation, Lineweaver-burk Plot, Cooperativity, Enzyme Substrate, Eadie-hofstee Diagram, Turnover Number, Substrate Channeling, Hanes-woolf Plot, Kinetic Perfection, Trypsin Inhibitor, Transition State Analog, Uncompetitive Inhibitor, Enzyme Activator, Immobilized Enzyme Esr, P50, Biochemical Cascade, Substrate Analog, Specificity Constant. Excerpt: ABTS In biochemistry , 2, 2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) or ABTS is chemical compound used to observe the reaction kinetics of specific enzymes . A common use for it is in the enzyme-linked immunosorbent assay (ELISA ) to detect for binding of molecules to each other. It is commonly used as a substrate with hydrogen peroxide for a peroxidase enzyme or alone with blue multicopper oxidase enzymes such as laccase or bilirubin oxidase . Its use allows the reaction kinetics of peroxidases themselves to be followed. In this way it also can be used to indirectly follow the reaction kinetics of any hydrogen peroxide -producing enzyme, or to simply quantify the amount of hydrogen peroxide in a sample. The formal reduction potentials for ABTS are high enough for it to act as an electron donor for the reduction of oxo species such as molecular oxygen and hydrogen peroxide, particularly at the less-extreme pH values encountered in biological catalysis. Under these conditions, the sulfonate groups are fully deprotonated and the mediator exists as a dianion. ABTS + e ABTS E° = 0.67 V vs SHE ABTS + e ABTS E° = 1.08 V vs SHE This compound is chosen because the enzyme facilitates the reaction with hydrogen peroxide, turning it into a green and soluble end-pr
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Enzyme Kinetics: Dissociation Constant, Law of Dilution, Allosteric Regulation, Cooperative Binding, Michaelis-menten Kinetics, Abt
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