Maud L. Menten coauthored the 1913 study of invertase that underlies Michaelis-Menten kinetics. The experiment followed changes in optical rotation as sucrose was hydrolysed, controlling acidity and accounting for the sugars' mutarotation. These controls mattered because the instrument observed a changing optical signal rather than the reaction rate directly. The resulting comparison of initial rates across substrate concentrations connected a measurable saturation curve to an enzyme-binding model.[ref]
Figure 1.
Portrait of Maud L. Menten
. Smithsonian Institution Archives portrait, Wikimedia Commons crop; the archive identifies the sitter. Source.

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