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Scatchard 图分析×米氏动力学×Schild 分析×
领域药理学药理学药理学
方法族Process / pipelineProcess / pipelineProcess / pipeline
起源年份194919131947
提出者George ScatchardLeonor Michaelis and Maud MentenHenry Schild
类型binding affinity measurementmechanistic modelantagonism quantification
开创性文献Scatchard, G. (1949). The attractions of proteins for small molecules and ions. Annals of the New York Academy of Sciences, 51(4), 660-672. DOI ↗Michaelis, L., & Menten, M. L. (1913). Die Kinetik der Invertinwirkung. Biochemische Zeitschrift, 49, 333-369. link ↗Schild, H. O. (1947). pA, a new scale for the measurement of drug antagonism. Journal of Physiology, 106(3), 337-357. DOI ↗
别名Scatchard plot, binding analysis, Kd determinationMM kinetics, Michaelis constant, VmaxSchild plot, pA2
相关323
摘要Scatchard analysis is a graphical method for determining ligand-receptor binding affinity (Kd) and binding capacity (Bmax) from binding data. Developed by George Scatchard in 1949, the Scatchard plot linearizes hyperbolic binding curves, enabling visual detection of multiple binding sites and quantitative parameter estimation.Michaelis-Menten kinetics describes the rate of enzyme-catalyzed reactions as a function of substrate concentration. Developed by Leonor Michaelis and Maud Menten in 1913, this foundational framework models enzyme catalysis through the rapid-equilibrium approximation and enables prediction of drug metabolism rates in pharmacokinetics.Schild analysis is a quantitative method for characterizing competitive receptor antagonism developed by Henry Schild in 1947. It uses dose-response curves in the presence and absence of antagonist to estimate the antagonist affinity constant (pA2), enabling standardized comparison of antagonist potency across drugs and experimental systems.
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ScholarGate方法对比: Scatchard Analysis · Michaelis-Menten Kinetics · Schild Analysis. 于 2026-06-19 检索自 https://scholargate.app/zh/compare