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Enzyme Kinetics Inversion of Sucrose

Abraham, J. Fisher, and P. Lofthus, Introduction to NMR Spectroscopy, Wiley, New York (1992). [Pg.271]

Binsch, Band-Shape Analysis, in L. M. Jackman and F. A. Cotton (eds.). Dynamic Nuclear Magnetic Resonance Spectroscopy, Academic Press, New York (1975). [Pg.271]

Sandstrom, Dynamic NMR Spectroscopy, Academic Press, New York (1982). [Pg.271]

A veiy important aspect of chemical kinetics is that dealing with the rates of enzyme-catalyzed reactions. Enzymes are a class of proteins that catalyze virtually all biochemical reactions. In this experiment we shall study the inversion of sucrose, as catalyzed by the enzyme invertase (/3-fractofuranidase) derived from yeast. The rate of the enzyme-catalyzed reaction will then be compared to that of the same reaction catalyzed by hydrogen ions. [Pg.271]

The basic mechanism for enzyme-catalyzed reactions was first proposed by Michaelis and Menten and confirmed by a study of the kinetics of the sucrose inversion. A simple reaction mechanism by which an enzyme converts a reactant S, usually called a substrate, into products P is... [Pg.271]

See other pages where Enzyme Kinetics Inversion of Sucrose is mentioned: [Pg.254]    [Pg.271]    [Pg.271]    [Pg.273]    [Pg.275]    [Pg.277]    [Pg.279]    [Pg.281]    [Pg.254]    [Pg.271]    [Pg.271]    [Pg.273]    [Pg.275]    [Pg.277]    [Pg.279]    [Pg.281]    [Pg.393]    [Pg.5]    [Pg.111]   


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