Michaelis-Menten kinetics Hanes-Woolf plot

On the other hand, the macrolides showed unusual enzymatic reactivity. Lipase PF-catalyzed polymerization of the macrolides proceeded much faster than that of 8-CL. The lipase-catalyzed polymerizability of lactones was quantitatively evaluated by Michaelis-Menten kinetics. For all monomers, linearity was observed in the Hanes-Woolf plot, indicating that the polymerization followed Michaehs-Menten kinetics. The V, (iaotone) and K,ax(iaotone)/ m(iaotone) values increased with the ring size of lactone, whereas the A (iactone) values scarcely changed. These data imply that the enzymatic polymerizability increased as a function of the ring size, and the large enzymatic polymerizability is governed mainly by the reachon rate hut not to the binding abilities, i.e., the reaction process of... 

A Lineweaver-Burk plot ( ) indicates that with D-glucose as the substrate, the enzyme obeys Michaelis-Menten kinetics with a Km value of 3.2 + 0.08 mM and a Vmax of 126.0 + 0.02 micromol/mg protein/min (Figure 11). Similar results were obtained by the direct linear plot (88), Hanes and Woolf ( ) or Eadie-Hofstee plots (90). All the kinetic data reported here and subsequently, were based on the initial rates of hydrogen peroxide formation... 

FIGURE 4.3 Hanes-Woolf plot of a reaction that follows Michaelis-Menten kinetics. Kinetic parameters are as defined previously. 

Fig. 6.6 Hanes-Woolf plot for Michaelis-Menten kinetics.

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