Maud Menten

Maud Leonora Menten (1879–1960) was a Canadian physician and biochemist who co-developed the Michaelis–Menten equation and advanced histochemistry and cancer research.

Leonor Michaelis: A German biochemist who studied enzyme kinetics and co-authored the 1913 paper with Maud Menten. Their joint work produced the equation most closely associated with Menten.
Michaelis–Menten kinetics: A model describing how the initial rate of an enzyme-catalyzed reaction depends on substrate concentration. It formalizes the enzyme-rate relationship Menten and Michaelis derived.
1913 Michaelis–Menten paper: A paper by Leonor Michaelis and Maud Menten that formulated a quantitative model of enzyme action. This publication presented the collaboration that made Menten’s name enduring in biochemistry.
Histochemistry: The study of the chemical composition and reactions of cells and tissues using microscopic methods. Menten developed techniques for locating chemical activity within tissue sections.
Lillian M. Menten: A Canadian physician and pathologist who collaborated with Maud Menten on histochemical research. Their work extended Menten’s research beyond enzyme kinetics.
Michaelis constant: The substrate concentration at which a Michaelis–Menten enzyme reaches half its maximum reaction rate. This parameter gives the equation a measurable marker of substrate dependence.
Invertase: An enzyme that hydrolyzes sucrose into glucose and fructose. Michaelis and Menten used invertase reactions to investigate enzyme kinetics.
Alkaline phosphatase: An enzyme that removes phosphate groups from molecules under alkaline conditions. Menten’s histochemical research included methods for visualizing enzyme activity in tissues.
James Bertram Collip: A Canadian biochemist and physician known for purifying insulin and contributing to endocrinology. Collip was a fellow Canadian medical scientist whose research intersected with Menten’s era.
Turnover number: The number of substrate molecules converted to product per enzyme molecule per unit time at saturation. It connects maximum reaction rate to the amount of enzyme present.

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