= L. Michaelis
{c}
<L. Michaelis> coauthored the 1913 <invertase> study with <Maud L. Menten>. Their interpretation connected the <substrate> dependence of reaction speed to reversible enzyme-substrate binding followed by conversion to product. At high <substrate> concentration, occupation of the finite <enzyme> population limits the rate, giving the saturation behavior associated with <Michaelis-Menten kinetics>.<The Kinetics of Invertase Action by L. Michaelis and Maud L. Menten>[Translated original, binding-equilibrium interpretation and the initial-rate dependence on sucrose concentration]{ref}
The original equilibrium-binding argument should be distinguished from the later quasi-steady-state derivation of the same rate-law shape. Fitting that shape alone does not distinguish every possible microscopic mechanism. https://digitalcommons.rockefeller.edu/faculty-members/56/[The Rockefeller Archive Center's identified 1946 portrait] records the scientist as Leonor Michaelis.
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