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. 1974 Oct;143(1):93–95. doi: 10.1042/bj1430093

A new method for determining the Michaelis constant

Felipe De Miguel Merino 1
PMCID: PMC1168356  PMID: 4464860

Abstract

A new method is described for evaluating the parameters Km and V in the Michaelis–Menten equation, and is illustrated with experimental data from the literature.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Hanes C. S. Studies on plant amylases: The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem J. 1932;26(5):1406–1421. doi: 10.1042/bj0261406. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. JOHANSEN G., LUMRY R. Statistical analysis of enzymic steady-state rate data. C R Trav Lab Carlsberg. 1961;32:185–214. [PubMed] [Google Scholar]
  3. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]

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